http://journals.iucr.org/d/journalhomepage.html Acta Crystallographica Section D: Biological Crystallography welcomes the submission of papers covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports on new protein structures are particularly encouraged, as are structure-function papers that could include crystallographic binding studies, or structural analysis of mutants or other modified forms of a known protein structure. The key criterion is that such papers should present new insights into biology, chemistry or structure. en-gb Copyright (c) 2013 International Union of Crystallography International Union of Crystallography International Union of Crystallography http://journals.iucr.org urn:issn:0907-4449 Acta Crystallographica Section D: Biological Crystallography welcomes the submission of papers covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports on new protein structures are particularly encouraged, as are structure-function papers that could include crystallographic binding studies, or structural analysis of mutants or other modified forms of a known protein structure. The key criterion is that such papers should present new insights into biology, chemistry or structure. text/html Acta Crystallographica Section D Biological Crystallography text daily 1 2002-01-01T00:00+00:00 med@iucr.org Acta Crystallographica Section D Biological Crystallography Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 http://journals.iucr.org/logos/rss10d.gif http://journals.iucr.org/d/journalhomepage.html Still image http://journals.iucr.org/d/services/forthcoming.html#cb5035 Magnesium bound to Trypanosoma brucei pyruvate kinase in the presence of the allosteric activator fructose bisphosphate, but absence of the substrate phosphoenolpyruvate is sequestered in a previously undescribed 'priming' position adjacent to the active site. In this way the enzyme is kept in a conformation with high affinity for the substrate. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Zhong et al. doi: International Union of Crystallography Magnesium bound to Trypanosoma brucei pyruvate kinase in the presence of the allosteric activator fructose bisphosphate, but absence of the substrate phosphoenolpyruvate is sequestered in a previously undescribed 'priming' position adjacent to the active site. In this way the enzyme is kept in a conformation with high affinity for the substrate. en Magnesium bound to Trypanosoma brucei pyruvate kinase in the presence of the allosteric activator fructose bisphosphate, but absence of the substrate phosphoenolpyruvate is sequestered in a previously undescribed 'priming' position adjacent to the active site. In this way the enzyme is kept in a conformation with high affinity for the substrate. text/html 'In crystallo' substrate binding triggers major domain movements and reveals magnesium as a co-activator of Trypanosoma brucei pyruvate kinase text http://journals.iucr.org/d/services/forthcoming.html#mn5031 Crystal structure analyses of the monooxygenase TetX in complex with tigecycline and minocycline support the observation that all clinically available tetracycline antibiotics can be inactivated by enzymatic hydroxylation. Molecular dynamics simulations of dioxygen diffusion and experimental xenon binding sites in TetX are compared with respect to putative dioxygen binding cavities and diffusion pathways. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Volkers et al. doi: International Union of Crystallography Crystal structure analyses of the monooxygenase TetX in complex with tigecycline and minocycline support the observation that all clinically available tetracycline antibiotics can be inactivated by enzymatic hydroxylation. Molecular dynamics simulations of dioxygen diffusion and experimental xenon binding sites in TetX are compared with respect to putative dioxygen binding cavities and diffusion pathways. en ANTIBIOTIC RESISTANCE; TIGECYCLINE; MINOCYCLINE; TETX; MONOOXYGENASE; XENON; DIOXYGEN DIFFUSION; MOLECULAR DYNAMICS; SIMULATION Crystal structure analyses of the monooxygenase TetX in complex with tigecycline and minocycline support the observation that all clinically available tetracycline antibiotics can be inactivated by enzymatic hydroxylation. Molecular dynamics simulations of dioxygen diffusion and experimental xenon binding sites in TetX are compared with respect to putative dioxygen binding cavities and diffusion pathways. text/html Putative dioxygen binding sites and recognition of tigecycline and minocycline in the tetracycline-degrading monooxygenase TetX text http://journals.iucr.org/d/services/forthcoming.html#ba5187 A processing pipeline for diffraction data acquired using the `serial crystallography' methodology with a free-electron laser source is described with reference to the crystallographic analysis suite CrystFEL and the pre-processing program Cheetah. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 White et al. doi:10.1107/S0907444913013620 International Union of Crystallography A processing pipeline for diffraction data acquired using the `serial crystallography' methodology with a free-electron laser source is described with reference to the crystallographic analysis suite CrystFEL and the pre-processing program Cheetah. en DATA PROCESSING; FREE-ELECTRON LASERS; SERIAL CRYSTALLOGRAPHY; CRYSTFEL; CHEETAH A processing pipeline for diffraction data acquired using the `serial crystallography' methodology with a free-electron laser source is described with reference to the crystallographic analysis suite CrystFEL and the pre-processing program Cheetah. text/html Crystallographic data processing for free-electron laser sources text http://journals.iucr.org/d/services/forthcoming.html#ba5197 Recent developments in X-ray crystallographic hardware related to structural biology research are presented and discussed. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Skarzynski doi:10.1107/S0907444913013619 International Union of Crystallography Recent developments in X-ray crystallographic hardware related to structural biology research are presented and discussed. en MACROMOLECULAR CRYSTALLOGRAPHY; X-RAY HARDWARE; DATA COLLECTION Recent developments in X-ray crystallographic hardware related to structural biology research are presented and discussed. text/html Collecting data in the home laboratory: evolution of X-ray sources, detectors and working practices text http://journals.iucr.org/d/services/forthcoming.html#mn5032 The crystal structure of Est25, a bacterial homolog of hormone-sensitive lipase (HSL) was determined at 1.49 Å resolution. Biochemical properties of Est25 were investigated to clarify the functional capacities of HSL and potential applications of Est25 in biotechnology. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Tri Duc Ngo et al. doi: International Union of Crystallography The crystal structure of Est25, a bacterial homolog of hormone-sensitive lipase (HSL) was determined at 1.49 Å resolution. Biochemical properties of Est25 were investigated to clarify the functional capacities of HSL and potential applications of Est25 in biotechnology. en The crystal structure of Est25, a bacterial homolog of hormone-sensitive lipase (HSL) was determined at 1.49 Å resolution. Biochemical properties of Est25 were investigated to clarify the functional capacities of HSL and potential applications of Est25 in biotechnology. text/html Structural and Functional Analyses of a Bacterial Homologue of Hormone-Sensitive Lipase from a Metagenomic Library text http://journals.iucr.org/d/services/forthcoming.html#ba5198 Strategies for phasing nucleic acid structures by molecular replacement, using both experimental and de novo designed models, are discussed. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Marco Marcia et al. doi: International Union of Crystallography Strategies for phasing nucleic acid structures by molecular replacement, using both experimental and de novo designed models, are discussed. en NUCLEIC ACID SEQUENCE HOMOLOGY; DE NOVO STRUCTURE DESIGN; LONG NON-CODING RNA; RNA STRUCTURE; HOMOLOGY MODELING; RCRANE Strategies for phasing nucleic acid structures by molecular replacement, using both experimental and de novo designed models, are discussed. text/html Solving nucleic acid structures by molecular replacement: examples from group II intron studies text http://journals.iucr.org/d/services/forthcoming.html#ba5199 This article gives an overview of techniques and procedures for efficient data collection at synchrotron sources. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Krojer et al. doi:10.1107/S0907444913013280 International Union of Crystallography This article gives an overview of techniques and procedures for efficient data collection at synchrotron sources. en DATA COLLECTION; DATA-COLLECTION STRATEGY; STRUCTURAL GENOMICS This article gives an overview of techniques and procedures for efficient data collection at synchrotron sources. text/html Squeezing the most from every crystal: the fine details of data collection text http://journals.iucr.org/d/services/forthcoming.html#ba5201 The use of molecular replacement in solving G protein-coupled receptors is discussed, with specific examples described in detail. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Andrew C. Kruse et al. doi: International Union of Crystallography The use of molecular replacement in solving G protein-coupled receptors is discussed, with specific examples described in detail. en MOLECULAR REPLACEMENT; G PROTEIN-COUPLED RECEPTOR; GPCR; MEMBRANE PROTEIN The use of molecular replacement in solving G protein-coupled receptors is discussed, with specific examples described in detail. text/html Applications of molecular replacement to G protein coupled receptors text http://journals.iucr.org/d/services/forthcoming.html#dz5284 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Stefania Correale et al. doi: International Union of Crystallography en CELL WALL; CRYSTAL STRUCTURE; PEPTIDOGLYCAN; TUBERCULOSIS. text/html Structures of free and inhibited forms of L,D-transpeptidase LdtMt1 from Mycobacterium tuberculosis text http://journals.iucr.org/d/services/forthcoming.html#mh5086 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Hai Minh Ta et al. doi: International Union of Crystallography en AMINOPEPTIDASE / PEPS / SUBSTRATE LENGTH SELECTIVITY / TRIPLE-SIEVED INTERLOCK MECHANISM text/html Structure-based elucidation of the regulatory mechanism for aminopeptidase activity text http://journals.iucr.org/d/services/forthcoming.html#mh5093 The crystal structure of a novel C-terminal dimerization domain of the cullin3 adaptor, SPOP, is reported. The dimerization interfaces of the SPOP BTB- and C-terminal domains act in tandem to generate high-order oligomers that enhance the ubiquitination of substrates. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Laura K. van Geersdaele et al. doi: International Union of Crystallography The crystal structure of a novel C-terminal dimerization domain of the cullin3 adaptor, SPOP, is reported. The dimerization interfaces of the SPOP BTB- and C-terminal domains act in tandem to generate high-order oligomers that enhance the ubiquitination of substrates. en POZ DOMAIN; BACK DOMAIN; E3 LIGASE; UBIQUITINATION The crystal structure of a novel C-terminal dimerization domain of the cullin3 adaptor, SPOP, is reported. The dimerization interfaces of the SPOP BTB- and C-terminal domains act in tandem to generate high-order oligomers that enhance the ubiquitination of substrates. text/html Structural Basis of High-Order Oligomerization of the Cullin3 Adaptor, SPOP text http://journals.iucr.org/d/services/forthcoming.html#cb5030 Structural studies of quinolinate synthase suggest a model for the enzyme substrate complex and an enzyme intermediate complex with a [4Fe-4S] cluster. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Erika V. Soriano et al. doi: International Union of Crystallography Structural studies of quinolinate synthase suggest a model for the enzyme substrate complex and an enzyme intermediate complex with a [4Fe-4S] cluster. en NAD BIOSYNTHESIS; IRON-SULFUR CLUSTER; GENE TRIPLICATION Structural studies of quinolinate synthase suggest a model for the enzyme substrate complex and an enzyme intermediate complex with a [4Fe-4S] cluster. text/html Active Site Models for Complexes of Quinolinate Synthase with Substrates and Intermediates text http://journals.iucr.org/d/services/forthcoming.html#dz5278 A systematic approach to the scaling and merging of data from multiple crystals in macromolecular crystallography is introduced and explained. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 James Foadi et al. doi: International Union of Crystallography A systematic approach to the scaling and merging of data from multiple crystals in macromolecular crystallography is introduced and explained. en ; ; ; A systematic approach to the scaling and merging of data from multiple crystals in macromolecular crystallography is introduced and explained. text/html Clustering procedures for the optimal selection of datasets from multiple crystals in macromolecular crystallography. text http://journals.iucr.org/d/services/forthcoming.html#kw5064 The crystal structures of the GluA2 LBD in complex with the positive allosteric modulator CX516 and its methyl substituted analogue Me-CX516 show that the binding modes are similar to that of aniracetam and CX614. This supports that CX516 affects receptor deactivation. The structures also show that there is limited space for substitutions at the piperidine ring of CX516. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Krintel et al. doi: International Union of Crystallography The crystal structures of the GluA2 LBD in complex with the positive allosteric modulator CX516 and its methyl substituted analogue Me-CX516 show that the binding modes are similar to that of aniracetam and CX614. This supports that CX516 affects receptor deactivation. The structures also show that there is limited space for substitutions at the piperidine ring of CX516. en IONOTROPIC GLUTAMATE RECEPTOR; GLUA2; CX516; POSITIVE ALLOSTERIC MODULATOR; LIGAND-BINDING DOMAIN. PDB REFERENCE; 4IY5 AND 4IY6 The crystal structures of the GluA2 LBD in complex with the positive allosteric modulator CX516 and its methyl substituted analogue Me-CX516 show that the binding modes are similar to that of aniracetam and CX614. This supports that CX516 affects receptor deactivation. The structures also show that there is limited space for substitutions at the piperidine ring of CX516. text/html Structural analysis of the positive AMPA receptor modulators CX516 and Me-CX516 in complex with the GluA2 ligand-binding domain text http://journals.iucr.org/d/services/forthcoming.html#wd5210 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Ruiz et al. doi: International Union of Crystallography en [BETA]-SANDWICH; HOMOLOGY; LECTIN; OLIGOMERISATION; PHYLOGENY text/html Fine-tuning of Proto-type Chicken Galectins: Crystal Structure of CG-2 and Structure-Activity Correlations text http://journals.iucr.org/d/services/forthcoming.html#dz5283 The first structure of the N-terminal domain of Mg2+ channel Mrs2 in monomeric form and a pentameric model of Mrs2 generated using the prokaryotic homologue CorA. Gating and metal sensing residues were proposed, based on the model and validated using mutational and functional studies in vivo. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Khan et al. doi: International Union of Crystallography The first structure of the N-terminal domain of Mg2+ channel Mrs2 in monomeric form and a pentameric model of Mrs2 generated using the prokaryotic homologue CorA. Gating and metal sensing residues were proposed, based on the model and validated using mutational and functional studies in vivo. en EUKARYOTIC MG2+ CHANNEL; MRS2; X-RAY CRYSTALLOGRAPHY; HYDROPHOBIC GATE; MAG-FURA 2 SPECTROFLUOROMETRY The first structure of the N-terminal domain of Mg2+ channel Mrs2 in monomeric form and a pentameric model of Mrs2 generated using the prokaryotic homologue CorA. Gating and metal sensing residues were proposed, based on the model and validated using mutational and functional studies in vivo. text/html Structural and Functional Characterization of the N-terminal Domain of Yeast Mg2+ Channel Mrs2 text http://journals.iucr.org/d/services/forthcoming.html#dz5282 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Oliviero Carugo et al. doi: International Union of Crystallography en text/html Half a century of Ramachandran plots text http://journals.iucr.org/d/services/forthcoming.html#ba5202 A brief overview, with examples, of the evolution of molecular replacement methods and models over the past few years is presented Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Giovanna Scapin doi: International Union of Crystallography A brief overview, with examples, of the evolution of molecular replacement methods and models over the past few years is presented en MOLECULAR REPLACEMENT; MODELS; ACCURACY; QUALITY A brief overview, with examples, of the evolution of molecular replacement methods and models over the past few years is presented text/html Molecular replacement then and now text http://journals.iucr.org/d/services/forthcoming.html#ba5203 The crystallographic steps towards the structure determination of a complete eukaryotic exosome complex bound to RNA are presented. Phasing of this 11-protein subunit complex was carried out via molecular replacement. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Makino and Conti doi: International Union of Crystallography The crystallographic steps towards the structure determination of a complete eukaryotic exosome complex bound to RNA are presented. Phasing of this 11-protein subunit complex was carried out via molecular replacement. en EXOSOME; MOLECULAR REPLACEMENT; MODEL BUILDING; RNA; NUCLEASE; RRP44 The crystallographic steps towards the structure determination of a complete eukaryotic exosome complex bound to RNA are presented. Phasing of this 11-protein subunit complex was carried out via molecular replacement. text/html Structure Determination of an 11-Subunit Exosome in Complex with RNA by Molecular Replacement text http://journals.iucr.org/d/services/forthcoming.html#ba5194 A comparison of X-ray diffraction and radiographic techniques for the location and characterization of protein crystals is demonstrated on membrane-protein crystals mounted within lipid cubic phase material. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Warren et al. doi:10.1107/S0907444913011359 International Union of Crystallography A comparison of X-ray diffraction and radiographic techniques for the location and characterization of protein crystals is demonstrated on membrane-protein crystals mounted within lipid cubic phase material. en MEMBRANE PROTEINS; LIPID CUBIC PHASE; MICRORADIOGRAPHY; MICROTOMOGRAPHY A comparison of X-ray diffraction and radiographic techniques for the location and characterization of protein crystals is demonstrated on membrane-protein crystals mounted within lipid cubic phase material. text/html Visualization of membrane-protein crystals in the lipid cubic phase using X-ray imaging text http://journals.iucr.org/d/services/forthcoming.html#mn5029 The crystal structure of full-length human CTNNBL1 reveals many unique structural features that establish CTNNBL1 as a distinct member of the armadillo-repeat protein family. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Huang et al. doi:10.1107/S0907444913011360 International Union of Crystallography The crystal structure of full-length human CTNNBL1 reveals many unique structural features that establish CTNNBL1 as a distinct member of the armadillo-repeat protein family. en ARMADILLO REPEAT; CTNNBL1; AID; NUCLEAR IMPORT The crystal structure of full-length human CTNNBL1 reveals many unique structural features that establish CTNNBL1 as a distinct member of the armadillo-repeat protein family. text/html Structure of full-length human CTNNBL1 reveals a distinct member of the armadillo-repeat protein family text http://journals.iucr.org/d/services/forthcoming.html#be5232 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Sjuts et al. doi:10.1107/S0907444913011323 International Union of Crystallography en O-DEMETHYLATION; COBALAMIN-BINDING PROTEIN; DESULFITOBACTERIUM HAFNIENSE text/html Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2 text http://journals.iucr.org/d/services/forthcoming.html#dw5049 The crystal structure of the SOCS2–elongin BC–Cul5(1–386) complex explains the specificity of Cul2 and Cul5 for elongin BC and their preferential association with Cul2 or Cul5 box-containing proteins. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Kim et al. doi:10.1107/S0907444913011220 International Union of Crystallography The crystal structure of the SOCS2–elongin BC–Cul5(1–386) complex explains the specificity of Cul2 and Cul5 for elongin BC and their preferential association with Cul2 or Cul5 box-containing proteins. en CULLIN-RING UBIQUITIN LIGASES; SOCS2-ELONGIN BC-CUL2/CUL5 COMPLEX; MOLECULAR ASSEMBLY; INTERSUBUNIT RECOGNITION The crystal structure of the SOCS2–elongin BC–Cul5(1–386) complex explains the specificity of Cul2 and Cul5 for elongin BC and their preferential association with Cul2 or Cul5 box-containing proteins. text/html Structural basis for intersubunit recognition in elongin BC–cullin 5–SOCS-box protein-ubiquitin ligase complexes text http://journals.iucr.org/d/services/forthcoming.html#kw5065 Structural studies of the protein encoded by orf12 of the clavulanic acid biosynthesis gene cluster from S. clavuligerus reveal a two-domain structure. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Valegård et al. doi:10.1107/S0907444913011013 International Union of Crystallography Structural studies of the protein encoded by orf12 of the clavulanic acid biosynthesis gene cluster from S. clavuligerus reveal a two-domain structure. en CLAVULANIC ACID BIOSYNTHESIS PATHWAY; ESTERASES; [BETA]-LACTAMASE FOLD; [BETA]-LACTAM ANTIBIOTICS; PENICILLIN-BINDING PROTEINS Structural studies of the protein encoded by orf12 of the clavulanic acid biosynthesis gene cluster from S. clavuligerus reveal a two-domain structure. text/html Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway text http://journals.iucr.org/d/services/forthcoming.html#be5230 The crystal structure of lumazine synthase from C. glabrata complexed with its catalytic product 6,7-dimethyl-8-(d-ribityl)lumazine is reported. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Shankar et al. doi:10.1107/S0907444913010949 International Union of Crystallography The crystal structure of lumazine synthase from C. glabrata complexed with its catalytic product 6,7-dimethyl-8-(d-ribityl)lumazine is reported. en CANDIDA GLABRATA; LUMAZINE SYNTHASE; 6,7-DIMETHYL-8-(D-RIBITYL)LUMAZINE; FUNGAL PATHOGENS The crystal structure of lumazine synthase from C. glabrata complexed with its catalytic product 6,7-dimethyl-8-(d-ribityl)lumazine is reported. text/html Catalysis product captured in lumazine synthase from the fungal pathogen Candida glabrata text http://journals.iucr.org/d/services/forthcoming.html#mh5087 The enzymatic and structural characterization of the drug target purine-specific nucleosidase from the pathogen T. brucei provides a rationale for the tight-binding inhibition by iminoribitol-based compounds. The binding of a metalorganic inhibitor to nucleoside hydrolases is reported for the first time, together with the structural basis of metal-mediated noncompetitive inhibition. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Giannese et al. doi:10.1107/S0907444913010792 International Union of Crystallography The enzymatic and structural characterization of the drug target purine-specific nucleosidase from the pathogen T. brucei provides a rationale for the tight-binding inhibition by iminoribitol-based compounds. The binding of a metalorganic inhibitor to nucleoside hydrolases is reported for the first time, together with the structural basis of metal-mediated noncompetitive inhibition. en PURINE NUCLEOSIDASES; TRYPANOSOMES; ENZYME-INHIBITOR COMPLEXES; NONCOMPETITIVE INHIBITION The enzymatic and structural characterization of the drug target purine-specific nucleosidase from the pathogen T. brucei provides a rationale for the tight-binding inhibition by iminoribitol-based compounds. The binding of a metalorganic inhibitor to nucleoside hydrolases is reported for the first time, together with the structural basis of metal-mediated noncompetitive inhibition. text/html Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor text http://journals.iucr.org/d/services/forthcoming.html#dz5276 Structure refinement with nonspherical scattering factors from the invariom database is performed on thiostrepton, a heavily modified hexadecapeptide with antibiotic activity. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Pröpper et al. doi:10.1107/S0907444913010664 International Union of Crystallography Structure refinement with nonspherical scattering factors from the invariom database is performed on thiostrepton, a heavily modified hexadecapeptide with antibiotic activity. en INVARIOM REFINEMENT; THIOSTREPTON Structure refinement with nonspherical scattering factors from the invariom database is performed on thiostrepton, a heavily modified hexadecapeptide with antibiotic activity. text/html Invariom refinement of a new monoclinic solvate of thiostrepton at 0.64 Å resolution text http://journals.iucr.org/d/services/forthcoming.html#mh5089 The crystal structure of the N-terminal part of T. thermophilus DnaJ unexpectedly showed an ordered GF domain and guided the design of a construct enabling the first structure determination of a complete DnaJ cochaperone molecule. By combining the crystal structures with spin-labelling EPR and cross-linking in solution, a dynamic view of this flexible molecule was developed. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Barends et al. doi:10.1107/S0907444913010640 International Union of Crystallography The crystal structure of the N-terminal part of T. thermophilus DnaJ unexpectedly showed an ordered GF domain and guided the design of a construct enabling the first structure determination of a complete DnaJ cochaperone molecule. By combining the crystal structures with spin-labelling EPR and cross-linking in solution, a dynamic view of this flexible molecule was developed. en MOLECULAR CHAPERONES; CRYSTAL DEHYDRATION; RADIATION-DAMAGE-INDUCED PHASING WITH ANOMALOUS SCATTERING; SINGLE-WAVELENGTH ANOMALOUS DIFFRACTION; ELECTRON PARAMAGNETIC RESONANCE; CROSS-LINKING; HYBRID STRUCTURE DETERMINATION The crystal structure of the N-terminal part of T. thermophilus DnaJ unexpectedly showed an ordered GF domain and guided the design of a construct enabling the first structure determination of a complete DnaJ cochaperone molecule. By combining the crystal structures with spin-labelling EPR and cross-linking in solution, a dynamic view of this flexible molecule was developed. text/html Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ text http://journals.iucr.org/d/services/forthcoming.html#dw5043 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Yu et al. doi:10.1107/S0907444913010457 International Union of Crystallography en PTP RECEPTOR TYPE Q; PROTEIN TYROSINE PHOSPHATASES text/html Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates text http://journals.iucr.org/d/services/forthcoming.html#mh5082 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Kang et al. doi:10.1107/S0907444913010196 International Union of Crystallography en PROCASPASE-7; CASPASE-7 ACTIVATION; INHIBITORS text/html Structural asymmetry of procaspase-7 bound to a specific inhibitor text http://journals.iucr.org/d/services/forthcoming.html#lv5037 The ribonucleotide-binding properties of Hfq were probed using crystallography. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Murina et al. doi:10.1107/S090744491301010X International Union of Crystallography The ribonucleotide-binding properties of Hfq were probed using crystallography. en HFQ; RNA-PROTEIN INTERACTIONS; RIBONUCLEOTIDE-PROTEIN COMPLEXES The ribonucleotide-binding properties of Hfq were probed using crystallography. text/html Hfq binds ribonucleotides in three different RNA-binding sites text http://journals.iucr.org/d/services/forthcoming.html#be5225 A novel three-chain nontoxic homologue of type II ribosome-inactivating proteins has been sequenced by mass spectrometry and its crystal structure has been determined. The evolutionary history of type II RIPs and the molecular basis for the loss of toxicity in some of them have been explored. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Sharma et al. doi:10.1107/S0907444913010020 International Union of Crystallography A novel three-chain nontoxic homologue of type II ribosome-inactivating proteins has been sequenced by mass spectrometry and its crystal structure has been determined. The evolutionary history of type II RIPs and the molecular basis for the loss of toxicity in some of them have been explored. en [BETA]-TREFOIL LECTINS; RIBOSOME-INACTIVATING PROTEINS; CLEAVED TOXIN CHAIN; MASS SPECTROMETRY A novel three-chain nontoxic homologue of type II ribosome-inactivating proteins has been sequenced by mass spectrometry and its crystal structure has been determined. The evolutionary history of type II RIPs and the molecular basis for the loss of toxicity in some of them have been explored. text/html The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs text http://journals.iucr.org/d/services/forthcoming.html#ba5186 An ultrasensitive Medipix2 detector allowed the collection of rotation electron-diffraction data from single three-dimensional protein nanocrystals for the first time. The data could be analysed using the standard X-ray crystallography programs MOSFLM and SCALA. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Nederlof et al. doi:10.1107/S0907444913009700 International Union of Crystallography An ultrasensitive Medipix2 detector allowed the collection of rotation electron-diffraction data from single three-dimensional protein nanocrystals for the first time. The data could be analysed using the standard X-ray crystallography programs MOSFLM and SCALA. en ELECTRON DIFFRACTION; ELECTRON MICROSCOPY; MEDIPIX2; MOSFLM; NANOCRYSTALS An ultrasensitive Medipix2 detector allowed the collection of rotation electron-diffraction data from single three-dimensional protein nanocrystals for the first time. The data could be analysed using the standard X-ray crystallography programs MOSFLM and SCALA. text/html A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals text http://journals.iucr.org/d/services/forthcoming.html#ba5196 Optical trapping has successfully been applied to select and mount microcrystals for subsequent X-ray diffraction experiments. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Wagner et al. doi:10.1107/S090744491300958X International Union of Crystallography Optical trapping has successfully been applied to select and mount microcrystals for subsequent X-ray diffraction experiments. en LASER TWEEZERS; OPTICAL TRAPPING; MICROCRYSTALS; CRYSTAL MANIPULATION; SAMPLE HOLDERS Optical trapping has successfully been applied to select and mount microcrystals for subsequent X-ray diffraction experiments. text/html Microcrystal manipulation with laser tweezers text http://journals.iucr.org/d/services/forthcoming.html#yt5052 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Sundlov & Gulick doi:10.1107/S0907444913009372 International Union of Crystallography en NONRIBOSOMAL PEPTIDE SYNTHETASES; ENTE; ENTB; ADENYLATION DOMAIN; CARRIER PROTEIN DOMAIN; NONCRYSTALLOGRAPHIC TRANSLATIONAL SYMMETRY text/html Structure determination of the functional domain interaction of a chimeric nonribosomal peptide synthetase from a challenging crystal with noncrystallographic translational symmetry text http://journals.iucr.org/d/services/forthcoming.html#lv5032 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Finfrock et al. doi:10.1107/S0907444913009335 International Union of Crystallography en SUBMICROMETRE LINE FOCUSING; X-RAY DAMAGE MITIGATION; PHOTOELECTRONS text/html Mitigation of X-ray damage in macromolecular crystallography by submicrometre line focusing text http://journals.iucr.org/d/services/forthcoming.html#lv5038 Structures of yeast Nit2 in complex with α-ketoglutarate and with oxaloacetate revealed the molecular-recognition mechanism of the enzyme for the first time, while that of the C169S mutant of yeast Nit2 showed a new ligand located in the catalytic cavity. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Liu et al. doi:10.1107/S0907444913009347 International Union of Crystallography Structures of yeast Nit2 in complex with α-ketoglutarate and with oxaloacetate revealed the molecular-recognition mechanism of the enzyme for the first time, while that of the C169S mutant of yeast Nit2 showed a new ligand located in the catalytic cavity. en NIT2; [ALPHA]-KETOGLUTARATE; OXALOACETATE; [ALPHA]-KETOGLUTARAMATE; [ALPHA]-KETOSUCCINAMATE; [OMEGA]-AMIDASES; HYDROLASES; ENZYME-LIGAND COMPLEXES Structures of yeast Nit2 in complex with α-ketoglutarate and with oxaloacetate revealed the molecular-recognition mechanism of the enzyme for the first time, while that of the C169S mutant of yeast Nit2 showed a new ligand located in the catalytic cavity. text/html Structures of enzyme–intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2 text http://journals.iucr.org/d/services/forthcoming.html#rr5036 Details of five very high-resolution accurate structures of bovine trypsin are compared in the context of the reproducibility of models obtained from crystals grown under identical conditions. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Liebschner et al. doi:10.1107/S0907444913009050 International Union of Crystallography Details of five very high-resolution accurate structures of bovine trypsin are compared in the context of the reproducibility of models obtained from crystals grown under identical conditions. en ATOMIC RESOLUTION; STRUCTURE COMPARISON; TRYPSIN; STRUCTURAL REPRODUCIBILITY Details of five very high-resolution accurate structures of bovine trypsin are compared in the context of the reproducibility of models obtained from crystals grown under identical conditions. text/html On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin text http://journals.iucr.org/d/services/forthcoming.html#be5229 Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Boone et al. doi:10.1107/S0907444913008743 International Union of Crystallography en HUMAN CARBONIC ANHYDRASE II; THERMAL STABILITY; DISULFIDE BRIDGES text/html Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond text http://journals.iucr.org/d/services/forthcoming.html#cb5027 The structures of tricyclic intermediates trapped in crystals of PhzG suggest a basis for the chemistry and promiscuity of the final steps of phenazine biosynthesis. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Xu et al. doi:10.1107/S0907444913008354 International Union of Crystallography The structures of tricyclic intermediates trapped in crystals of PhzG suggest a basis for the chemistry and promiscuity of the final steps of phenazine biosynthesis. en ANTIBIOTICS; HYDRIDE TRANSFER; REACTION MECHANISM; FLAVINS; PDXH The structures of tricyclic intermediates trapped in crystals of PhzG suggest a basis for the chemistry and promiscuity of the final steps of phenazine biosynthesis. text/html Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis text http://journals.iucr.org/d/services/forthcoming.html#dz5277 MAIN is interactive software designed to interactively perform the complex tasks of macromolecular crystal structure determination and validation. The features of MAIN and its tools for electron-density map calculations, model building, refinement in real and reciprocal space, and validation exploiting noncrystallographic symmetry in single and multiple crystal forms are presented. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Turk doi:10.1107/S0907444913008408 International Union of Crystallography MAIN is interactive software designed to interactively perform the complex tasks of macromolecular crystal structure determination and validation. The features of MAIN and its tools for electron-density map calculations, model building, refinement in real and reciprocal space, and validation exploiting noncrystallographic symmetry in single and multiple crystal forms are presented. en MOLECULAR MODELLING; MOLECULAR GRAPHICS; MACROMOLECULAR CRYSTAL STRUCTURE DETERMINATION; MAP CALCULATION; COMPUTER PROGRAMS MAIN is interactive software designed to interactively perform the complex tasks of macromolecular crystal structure determination and validation. The features of MAIN and its tools for electron-density map calculations, model building, refinement in real and reciprocal space, and validation exploiting noncrystallographic symmetry in single and multiple crystal forms are presented. text/html MAIN software for density averaging, model building, structure refinement and validation text http://journals.iucr.org/d/services/forthcoming.html#gm5022 The crystal structure of HP1028, a protein from the human pathogen H. pylori, demonstrates that it belongs to the lipocalin family. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Barison et al. doi:10.1107/S0907444913008160 International Union of Crystallography The crystal structure of HP1028, a protein from the human pathogen H. pylori, demonstrates that it belongs to the lipocalin family. en HELICOBACTER PYLORI; LIPOCALINS; BINDING PROTEINS; CHEMOTAXIS The crystal structure of HP1028, a protein from the human pathogen H. pylori, demonstrates that it belongs to the lipocalin family. text/html Protein HP1028 from the human pathogen Helicobacter pylori belongs to the lipocalin family text http://journals.iucr.org/d/services/forthcoming.html#dz5280 The crystal structure of an ATP-independent LonC protease revealed a proteolytic chamber with two open axial pores. A LonC-specific N-­terminal coil tethers the AAA+ and protease domains together. Structures with covalent inhibitors bound to the proteolytic active sites provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved Lon proteolytic chamber. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Liao et al. doi:10.1107/S0907444913008214 International Union of Crystallography The crystal structure of an ATP-independent LonC protease revealed a proteolytic chamber with two open axial pores. A LonC-specific N-­terminal coil tethers the AAA+ and protease domains together. Structures with covalent inhibitors bound to the proteolytic active sites provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved Lon proteolytic chamber. en INHIBITORS; LONC; LON PROTEASES The crystal structure of an ATP-independent LonC protease revealed a proteolytic chamber with two open axial pores. A LonC-specific N-­terminal coil tethers the AAA+ and protease domains together. Structures with covalent inhibitors bound to the proteolytic active sites provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved Lon proteolytic chamber. text/html Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors text http://journals.iucr.org/d/services/forthcoming.html#dz5281 Ultrahigh-resolution crystal structures of metal complexes of self-complementary Z-DNA with the sequence d(CG)3 revealed different coordination patterns for Mn2+ (octahedral) and Zn2+ (octahedral and tetrahedral) cations. The complete sperminium cation is visible in electron density in the Mn2+ structure, while in the Zn2+ structure it is partly disordered in unison with fragments of the DNA molecule. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Drozdzal et al. doi:10.1107/S0907444913007798 International Union of Crystallography Ultrahigh-resolution crystal structures of metal complexes of self-complementary Z-DNA with the sequence d(CG)3 revealed different coordination patterns for Mn2+ (octahedral) and Zn2+ (octahedral and tetrahedral) cations. The complete sperminium cation is visible in electron density in the Mn2+ structure, while in the Zn2+ structure it is partly disordered in unison with fragments of the DNA molecule. en Z-DNA; D(CG)3; MN2+; ZN2+ Ultrahigh-resolution crystal structures of metal complexes of self-complementary Z-DNA with the sequence d(CG)3 revealed different coordination patterns for Mn2+ (octahedral) and Zn2+ (octahedral and tetrahedral) cations. The complete sperminium cation is visible in electron density in the Mn2+ structure, while in the Zn2+ structure it is partly disordered in unison with fragments of the DNA molecule. text/html Ultrahigh-resolution crystal structures of Z-DNA in complex with Mn2+ and Zn2+ ions text http://journals.iucr.org/d/services/forthcoming.html#yt5051 The crystal structure of the C-terminal peptide of secretin bound to the surface of its cognate pilotin reveals interactions that are essential for the assembly of a functional type II secretion system in D. dadantii and related secretion systems. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Rehman et al. doi:10.1107/S0907444913007658 International Union of Crystallography The crystal structure of the C-terminal peptide of secretin bound to the surface of its cognate pilotin reveals interactions that are essential for the assembly of a functional type II secretion system in D. dadantii and related secretion systems. en TYPE II SECRETION SYSTEM; PILOTIN; SECRETIN; SECRETIN-PILOTIN COMPLEX The crystal structure of the C-terminal peptide of secretin bound to the surface of its cognate pilotin reveals interactions that are essential for the assembly of a functional type II secretion system in D. dadantii and related secretion systems. text/html Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin text http://journals.iucr.org/d/services/forthcoming.html#be5226 Structures of the B. subtilis dUTPases in a novel complex with dU–PPi–Mg2+ and in complex with dUMP provide insights into the mechanism and identify features unique to the B. subtilis enzymes. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 García-Nafría et al. doi:10.1107/S090744491300735X International Union of Crystallography Structures of the B. subtilis dUTPases in a novel complex with dU–PPi–Mg2+ and in complex with dUMP provide insights into the mechanism and identify features unique to the B. subtilis enzymes. en BACILLUS SUBTILIS; DUTPASES; ENZYME MECHANISM; DU-PPI-MG2+ COMPLEX; TRANSITION-STATE PSEUDO-MIMIC Structures of the B. subtilis dUTPases in a novel complex with dU–PPi–Mg2+ and in complex with dUMP provide insights into the mechanism and identify features unique to the B. subtilis enzymes. text/html Tying down the arm in Bacillus dUTPase: structure and mechanism text http://journals.iucr.org/d/services/forthcoming.html#mn5024 The crystal structure of SspCA, a novel `extremo-α-carbonic anhydrase', is described, providing an elucidation of the factors responsible for its function at high temperature. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Di Fiore et al. doi:10.1107/S0907444913007208 International Union of Crystallography The crystal structure of SspCA, a novel `extremo-α-carbonic anhydrase', is described, providing an elucidation of the factors responsible for its function at high temperature. en [ALPHA]-CARBONIC ANHYDRASES; SULFURIHYDROGENIBIUM YELLOWSTONENSE YO3AOP1; THERMOSTABILITY The crystal structure of SspCA, a novel `extremo-α-carbonic anhydrase', is described, providing an elucidation of the factors responsible for its function at high temperature. text/html X-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 text http://journals.iucr.org/d/services/forthcoming.html#mh5090 New programs for automated nucleic acid structure refinement, NAFIT and NABUILD, are described. They fit and extend the nucleic acid model and work with the automated iterative refinement system LAFIRE. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Yamashita et al. doi:10.1107/S0907444913007191 International Union of Crystallography New programs for automated nucleic acid structure refinement, NAFIT and NABUILD, are described. They fit and extend the nucleic acid model and work with the automated iterative refinement system LAFIRE. en LAFIRE; AUTOMATIC REFINEMENT; REAL-SPACE REFINEMENT; NUCLEIC ACID MODEL BUILDING; NUCLEIC ACID MODEL FITTING New programs for automated nucleic acid structure refinement, NAFIT and NABUILD, are described. They fit and extend the nucleic acid model and work with the automated iterative refinement system LAFIRE. text/html New model-fitting and model-completion programs for automated iterative nucleic acid refinement text http://journals.iucr.org/d/services/forthcoming.html#lv5030 This study underscores the plasticity of the multidrug-binding pocket in MarR proteins and may help for the understanding of the antimicrobial resistance mechanism in pathogens. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Chang et al. doi:10.1107/S0907444913007117 International Union of Crystallography This study underscores the plasticity of the multidrug-binding pocket in MarR proteins and may help for the understanding of the antimicrobial resistance mechanism in pathogens. en MULTIPLE DRUG RESISTANCE; BIOFILMS; TRANSCRIPTION REGULATION; DNA BINDING; ANTIBIOTICS This study underscores the plasticity of the multidrug-binding pocket in MarR proteins and may help for the understanding of the antimicrobial resistance mechanism in pathogens. text/html Structural analysis of the antibiotic-recognition mechanism of MarR proteins text http://journals.iucr.org/d/services/forthcoming.html#tz5028 Surface-residue mutagenesis and cocrystallization with Fab fragments, Fynomers or Xaperones were used to obtain the first high-resolution crystal structures of BACE2. These map the conformational space accessible to this potential drug target. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Banner et al. doi:10.1107/S0907444913006574 International Union of Crystallography Surface-residue mutagenesis and cocrystallization with Fab fragments, Fynomers or Xaperones were used to obtain the first high-resolution crystal structures of BACE2. These map the conformational space accessible to this potential drug target. en PROTEIN CRYSTALLIZATION; ANTIBODIES; DRUG DISCOVERY AND DESIGN Surface-residue mutagenesis and cocrystallization with Fab fragments, Fynomers or Xaperones were used to obtain the first high-resolution crystal structures of BACE2. These map the conformational space accessible to this potential drug target. text/html Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones text http://journals.iucr.org/d/services/forthcoming.html#en5538 The crystal structures of the eubacterial translation initiation factor 2 in apo form and with bound GDP and GTP reveal conformational changes upon nucleotide binding and hydrolysis, notably of the catalytically important histidine in the switch II region. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Simonetti et al. doi:10.1107/S0907444913006422 International Union of Crystallography The crystal structures of the eubacterial translation initiation factor 2 in apo form and with bound GDP and GTP reveal conformational changes upon nucleotide binding and hydrolysis, notably of the catalytically important histidine in the switch II region. en TRANSLATION INITIATION FACTOR 2; THERMUS THERMOPHILUS; GTP; GDP The crystal structures of the eubacterial translation initiation factor 2 in apo form and with bound GDP and GTP reveal conformational changes upon nucleotide binding and hydrolysis, notably of the catalytically important histidine in the switch II region. text/html Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms text http://journals.iucr.org/d/services/forthcoming.html#nj5150 The bound structure of a novel HIV-1 capsid-assembly inhibitor describes a unique inhibitor-binding site on the capsid N-terminal domain. Moreover, use of this inhibitor as a crystallization tool greatly improved the success rate of capsid N-terminal domain ternary cocrystallizations via compound-mediated synthetic dimerization. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Lemke et al. doi:10.1107/S0907444913006409 International Union of Crystallography The bound structure of a novel HIV-1 capsid-assembly inhibitor describes a unique inhibitor-binding site on the capsid N-terminal domain. Moreover, use of this inhibitor as a crystallization tool greatly improved the success rate of capsid N-terminal domain ternary cocrystallizations via compound-mediated synthetic dimerization. en HIV-1; CAPSID-ASSEMBLY INHIBITOR; COCRYSTALLIZATION; DIMERIZATION The bound structure of a novel HIV-1 capsid-assembly inhibitor describes a unique inhibitor-binding site on the capsid N-terminal domain. Moreover, use of this inhibitor as a crystallization tool greatly improved the success rate of capsid N-terminal domain ternary cocrystallizations via compound-mediated synthetic dimerization. text/html A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallization via compound-mediated dimerization text http://journals.iucr.org/d/services/forthcoming.html#xb5068 ps-2-HAD catalyses both l- and d- substrates, showing similar overall folding to l-HADs but completely different to the only structurally characterised dl-2-HAD enzyme. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Hou et al. doi:10.1107/S0907444913006021 International Union of Crystallography ps-2-HAD catalyses both l- and d- substrates, showing similar overall folding to l-HADs but completely different to the only structurally characterised dl-2-HAD enzyme. en 2-HALOACID DEHALOGENASES; MUTATION; ENZYMATIC ACTIVITY ps-2-HAD catalyses both l- and d- substrates, showing similar overall folding to l-HADs but completely different to the only structurally characterised dl-2-HAD enzyme. text/html Structure of 2-haloacid dehalogenase from Pseudomonas syringae pv. tomato DC3000 text http://journals.iucr.org/d/services/forthcoming.html#kw5061 The X-ray crystal structure of an outer surface protein BBA64 from the Lyme disease agent B. burgdorferi which is necessary to cause the disease is reported and compared with that of the homologous protein CspA from B. burgdorferi. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Brangulis et al. doi:10.1107/S0907444913005726 International Union of Crystallography The X-ray crystal structure of an outer surface protein BBA64 from the Lyme disease agent B. burgdorferi which is necessary to cause the disease is reported and compared with that of the homologous protein CspA from B. burgdorferi. en LYME BORRELIOSIS; IXODES TICKS; HOMOLOGOUS PROTEINS; LYME DISEASE THERAPY; OUTER SURFACE PROTEINS The X-ray crystal structure of an outer surface protein BBA64 from the Lyme disease agent B. burgdorferi which is necessary to cause the disease is reported and compared with that of the homologous protein CspA from B. burgdorferi. text/html Structure of an outer surface lipoprotein BBA64 from the Lyme disease agent Borrelia burgdorferi which is critical to ensure infection after a tick bite text http://journals.iucr.org/d/services/forthcoming.html#be5227 The putative methyltransferase CmoA is involved in the nucleoside modification of transfer RNA. X-ray crystallography and mass spectrometry are used to show that it contains a novel SAM derivative, S-adenosyl-S-carboxymethyl-l-homocysteine, in which the donor methyl group is replaced by a carboxymethyl group. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Byrne et al. doi:10.1107/S0907444913004939 International Union of Crystallography The putative methyltransferase CmoA is involved in the nucleoside modification of transfer RNA. X-ray crystallography and mass spectrometry are used to show that it contains a novel SAM derivative, S-adenosyl-S-carboxymethyl-l-homocysteine, in which the donor methyl group is replaced by a carboxymethyl group. en SCM-SAH; ESCHERICHIA COLI; PUTATIVE TRNA-MODIFICATION ENZYME; CMO5U BIOSYNTHESIS The putative methyltransferase CmoA is involved in the nucleoside modification of transfer RNA. X-ray crystallography and mass spectrometry are used to show that it contains a novel SAM derivative, S-adenosyl-S-carboxymethyl-l-homocysteine, in which the donor methyl group is replaced by a carboxymethyl group. text/html S-Adenosyl-S-carboxymethyl-l-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA text http://journals.iucr.org/d/services/forthcoming.html#mh5076 This study presents crystal structures of the catalytic domain of human DUSP26 and a catalytically inactive mutant at 1.67 and 2.20 Å resolution, respectively. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Won et al. doi:10.1107/S0907444913004770 International Union of Crystallography This study presents crystal structures of the catalytic domain of human DUSP26 and a catalytically inactive mutant at 1.67 and 2.20 Å resolution, respectively. en PTP; DUSP26; CATALYTIC DOMAIN; DOMAIN SWAPPING This study presents crystal structures of the catalytic domain of human DUSP26 and a catalytically inactive mutant at 1.67 and 2.20 Å resolution, respectively. text/html High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26 text http://journals.iucr.org/d/services/forthcoming.html#dw5037 The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Krishnan et al. doi:10.1107/S0907444913004642 International Union of Crystallography The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. en TIP PILINS; GBS104; PILI ASSEMBLY; GROUP B STREPTOCOCCUS The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. text/html Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions text http://journals.iucr.org/d/services/forthcoming.html#mh5085 The 2.4 Å resolution crystal structure of the H. marismortui large ribosomal subunit has been re-refined; the structures of r-proteins P0 and P1 were visualized in part and r-protein LX and helix 76 of the 23S rRNA were localized. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Gabdulkhakov et al. doi:10.1107/S0907444913004745 International Union of Crystallography The 2.4 Å resolution crystal structure of the H. marismortui large ribosomal subunit has been re-refined; the structures of r-proteins P0 and P1 were visualized in part and r-protein LX and helix 76 of the 23S rRNA were localized. en ARCHAEAL RIBOSOME; 50S RIBOSOMAL SUBUNIT; P STALK; P0; L11; LX; HALOARCULA MARISMORTUI The 2.4 Å resolution crystal structure of the H. marismortui large ribosomal subunit has been re-refined; the structures of r-proteins P0 and P1 were visualized in part and r-protein LX and helix 76 of the 23S rRNA were localized. text/html Revisiting the Haloarcula marismortui 50S ribosomal subunit model text http://journals.iucr.org/d/services/forthcoming.html#rr5034 A computer simulation was created for a modulated protein structure along with structure factors in a periodic supercell and in superspace for the purpose of developing and validating software modifications that will be used to solve and refine modulated protein crystals. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Lovelace et al. doi:10.1107/S0907444913004630 International Union of Crystallography A computer simulation was created for a modulated protein structure along with structure factors in a periodic supercell and in superspace for the purpose of developing and validating software modifications that will be used to solve and refine modulated protein crystals. en PROTEIN; MODULATED STRUCTURES; SATELLITE REFLECTIONS; Q VECTORS; AVERAGE STRUCTURE; DISORDER; SUPERCELLS; SUPERSPACE A computer simulation was created for a modulated protein structure along with structure factors in a periodic supercell and in superspace for the purpose of developing and validating software modifications that will be used to solve and refine modulated protein crystals. text/html Simulation of modulated protein crystal structure and diffraction data in a supercell and in superspace text http://journals.iucr.org/d/services/forthcoming.html#mn5025 The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Squires et al. doi:10.1107/S0907444913004617 International Union of Crystallography The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV. en TRIATOMA VIRUS; TRV; CRIPAVIRUS; DICISTROVIRIDAE; VIRUS STRUCTURE; X-RAY CRYSTALLOGRAPHY The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV. text/html Structure of the Triatoma virus capsid text http://journals.iucr.org/d/services/forthcoming.html#cb5023 The crystal structure of starch synthase I from barley was refined to 2.7 Å resolution. It includes a regulatory disulfide and a bound oligosaccharide. Activity assays were performed on several mutants. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Cuesta-Seijo et al. doi:10.1107/S090744491300440X International Union of Crystallography The crystal structure of starch synthase I from barley was refined to 2.7 Å resolution. It includes a regulatory disulfide and a bound oligosaccharide. Activity assays were performed on several mutants. en STARCH SYNTHASES; BARLEY; DISULFIDES; MALTOOLIGOSACCHARIDE-BINDING SITES The crystal structure of starch synthase I from barley was refined to 2.7 Å resolution. It includes a regulatory disulfide and a bound oligosaccharide. Activity assays were performed on several mutants. text/html Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity text http://journals.iucr.org/d/services/forthcoming.html#mn5020 The design, validation, proof of mechanism and exploitation of a surface-entropy reduction mutant to solve the structure of the benchmark inhibitor Nutlin-3a bound to the cancer drug-discovery target MDM2 are reported. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Anil et al. doi:10.1107/S0907444913004459 International Union of Crystallography The design, validation, proof of mechanism and exploitation of a surface-entropy reduction mutant to solve the structure of the benchmark inhibitor Nutlin-3a bound to the cancer drug-discovery target MDM2 are reported. en MDM2; P53; NUTLIN-3A; SURFACE-ENTROPY REDUCTION; MUTANT VALIDATION The design, validation, proof of mechanism and exploitation of a surface-entropy reduction mutant to solve the structure of the benchmark inhibitor Nutlin-3a bound to the cancer drug-discovery target MDM2 are reported. text/html The structure of an MDM2–Nutlin-3a complex solved by the use of a validated MDM2 surface-entropy reduction mutant text http://journals.iucr.org/d/services/forthcoming.html#cb5026 Structures of the EAL domain of the E. coli direct oxygen sensor show the active site in a nonproductive conformation that has implications for the regulatory mechanism. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Tarnawski et al. doi:10.1107/S0907444913004423 International Union of Crystallography Structures of the EAL domain of the E. coli direct oxygen sensor show the active site in a nonproductive conformation that has implications for the regulatory mechanism. en EAL DOMAINS; PHOSPHODIESTERASES; CYCLIC DI-GMP; DOSP; DIRECT OXYGEN SENSORS; ESCHERICHIA COLI Structures of the EAL domain of the E. coli direct oxygen sensor show the active site in a nonproductive conformation that has implications for the regulatory mechanism. text/html Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor text http://journals.iucr.org/d/services/forthcoming.html#mn5023 Here, the re-refinement of the structure of the vault particle by incorporating the high-resolution information available for the R1–7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Casañas et al. doi:10.1107/S0907444913004472 International Union of Crystallography Here, the re-refinement of the structure of the vault particle by incorporating the high-resolution information available for the R1–7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported. en VAULT; RIBONUCLEOPROTEINS; DEFORMABLE ELASTIC NETWORK; REFINEMENT Here, the re-refinement of the structure of the vault particle by incorporating the high-resolution information available for the R1–7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported. text/html New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach text http://journals.iucr.org/d/services/forthcoming.html#lv5033 The VLD approach has been integrated into a molecular-replacement pipeline for automatic protein crystal structure solution. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Carrozzini et al. doi:10.1107/S0907444913004435 International Union of Crystallography The VLD approach has been integrated into a molecular-replacement pipeline for automatic protein crystal structure solution. en VLD; MOLECULAR REPLACEMENT; PHASING; AUTOMATED STRUCTURE SOLUTION The VLD approach has been integrated into a molecular-replacement pipeline for automatic protein crystal structure solution. text/html The use of VLD (vive la difference) in the molecular-replacement approach: a pipeline text http://journals.iucr.org/d/services/forthcoming.html#lv5026 The Glu43Ala/Phe81Ala mutation in binase prevents dimerization of the enzyme and improves its catalytic activity and cytotoxicity. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Mitkevich et al. doi:10.1107/S0907444913004046 International Union of Crystallography The Glu43Ala/Phe81Ala mutation in binase prevents dimerization of the enzyme and improves its catalytic activity and cytotoxicity. en RIBONUCLEASES; BINASE; SITE-DIRECTED MUTAGENESIS; ENZYMATIC ACTIVITY; CYTOTOXICITY The Glu43Ala/Phe81Ala mutation in binase prevents dimerization of the enzyme and improves its catalytic activity and cytotoxicity. text/html Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant text http://journals.iucr.org/d/services/forthcoming.html#lv5028 The yellow fluorescent protein phiYFPv with improved folding has been developed from the spectrally identical wild-type phiYFP found in the marine jellyfish Phialidium. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Pletneva et al. doi:10.1107/S0907444913004034 International Union of Crystallography The yellow fluorescent protein phiYFPv with improved folding has been developed from the spectrally identical wild-type phiYFP found in the marine jellyfish Phialidium. en YELLOW FLUORESCENT PROTEIN; PHIALIDIUM; STRUCTURE-FUNCTION RELATIONSHIP; CHROMOPHORES; OLIGOMERIC STRUCTURE; INTERSUBUNIT SURFACE The yellow fluorescent protein phiYFPv with improved folding has been developed from the spectrally identical wild-type phiYFP found in the marine jellyfish Phialidium. text/html Yellow fluorescent protein phiYFPv (Phialidium): structure and structure-based mutagenesis text http://journals.iucr.org/d/services/forthcoming.html#ba5185 Hardware and software solutions for MX data-collection strategies using the EMBL/ESRF miniaturized multi-axis goniometer head are presented. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Brockhauser et al. doi:10.1107/S0907444913003880 International Union of Crystallography Hardware and software solutions for MX data-collection strategies using the EMBL/ESRF miniaturized multi-axis goniometer head are presented. en KAPPA GONIOMETER; CRYSTAL ALIGNMENT; DATA-COLLECTION STRATEGIES Hardware and software solutions for MX data-collection strategies using the EMBL/ESRF miniaturized multi-axis goniometer head are presented. text/html The use of a mini-κ goniometer head in macromolecular crystallography diffraction experiments text http://journals.iucr.org/d/services/forthcoming.html#be5218 The crystal structures of two circularly permuted streptavidins probe the role of a flexible loop in the tight binding of biotin. Molecular-dynamics calculations for one of the mutants suggests that increased fluctuations in a hydrogen bond between the protein and biotin are associated with cleavage of the binding loop. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Le Trong et al. doi:10.1107/S0907444913003855 International Union of Crystallography The crystal structures of two circularly permuted streptavidins probe the role of a flexible loop in the tight binding of biotin. Molecular-dynamics calculations for one of the mutants suggests that increased fluctuations in a hydrogen bond between the protein and biotin are associated with cleavage of the binding loop. en BIOTIN-BINDING PROTEIN; BIOTIN; CIRCULAR PERMUTATION The crystal structures of two circularly permuted streptavidins probe the role of a flexible loop in the tight binding of biotin. Molecular-dynamics calculations for one of the mutants suggests that increased fluctuations in a hydrogen bond between the protein and biotin are associated with cleavage of the binding loop. text/html Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin text http://journals.iucr.org/d/services/forthcoming.html#mv5084 High-resolution powder X-ray diffraction data have been collected to reveal the T6 hexameric insulin form and a novel approach for refining protein structures using powder diffraction data is presented. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Margiolaki et al. doi:10.1107/S0907444913003867 International Union of Crystallography High-resolution powder X-ray diffraction data have been collected to reveal the T6 hexameric insulin form and a novel approach for refining protein structures using powder diffraction data is presented. en POWDER DIFFRACTION; T6 BOVINE INSULIN; SYNCHROTRON RADIATION; RIETVELD ANALYSIS High-resolution powder X-ray diffraction data have been collected to reveal the T6 hexameric insulin form and a novel approach for refining protein structures using powder diffraction data is presented. text/html High-resolution powder X-ray data reveal the T6 hexameric form of bovine insulin text http://journals.iucr.org/d/services/forthcoming.html#dw5039 Crystal structures of the BAG proteins from A. thaliana have been solved at high resolution. Structural and functional data provide evidence of an Hsp70/Hsc70 nucleotide-exchange factor function for these plant BAG proteins. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Fang et al. doi:10.1107/S0907444913003624 International Union of Crystallography Crystal structures of the BAG proteins from A. thaliana have been solved at high resolution. Structural and functional data provide evidence of an Hsp70/Hsc70 nucleotide-exchange factor function for these plant BAG proteins. en BAG PROTEINS; HSC70; UBIQUITIN-LIKE DOMAINS; PROGRAMMED CELL DEATH Crystal structures of the BAG proteins from A. thaliana have been solved at high resolution. Structural and functional data provide evidence of an Hsp70/Hsc70 nucleotide-exchange factor function for these plant BAG proteins. text/html Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana text http://journals.iucr.org/d/services/forthcoming.html#lv5035 The X-ray crystal structure of geodin is reported. Copyright (c) 2013 International Union of Crystallography urn:issn:0907-4449 Vergara et al. doi:10.1107/S0907444913003569 International Union of Crystallography The X-ray crystal structure of geodin is reported. en CRYSTALLINS; ATOMIC RESOLUTION; CALCIUM BINDING; DOMAIN INTERACTIONS; FOLDING; GREEK-KEY MOTIF; TYR CORNER; TRP CORNER The X-ray crystal structure of geodin is reported. text/html A novel interdomain interface in crystallins: structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 Å resolution text