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. Papers on crystallographic methods should be oriented towards biological crystallography, and may include new approaches to any aspect of structure determination or analysis. Papers on the crystallization of biological molecules will be accepted providing that these focus on new methods or other features that are of general importance or applicability. en-gb Copyright (c) 2012 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. Papers on crystallographic methods should be oriented towards biological crystallography, and may include new approaches to any aspect of structure determination or analysis. Papers on the crystallization of biological molecules will be accepted providing that these focus on new methods or other features that are of general importance or applicability. 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) 2012 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#dz5256 A method for experimental phasing by segmenting a large dataset into sub-datasets for radiation damage induced phasing (RIP) is presented. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 de Sanctis and Nanao doi: International Union of Crystallography A method for experimental phasing by segmenting a large dataset into sub-datasets for radiation damage induced phasing (RIP) is presented. en RIP; EXPERIMENTAL PHASING; SYNCHROTRON RADIATION; SUBSTRUCTURE DETERMINATION A method for experimental phasing by segmenting a large dataset into sub-datasets for radiation damage induced phasing (RIP) is presented. text/html Segmenting datasets for RIP text http://journals.iucr.org/d/services/forthcoming.html#xb5052 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Cheng Dong et al. doi: International Union of Crystallography en BAM COMPLEX; OMPS; LPS; POTRA DOMAIN text/html The structure of Escherichia coli BamB and its interaction with POTRA domains of BamA text http://journals.iucr.org/d/services/forthcoming.html#en5497 PDB References: 4agr, 4agv, 4agg The structure of a tetrameric sponge galectin suggests a basis for glutamate receptor potentiation. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Douglas M. Freymann et al. doi: International Union of Crystallography PDB References: 4agr, 4agv, 4agg The structure of a tetrameric sponge galectin suggests a basis for glutamate receptor potentiation. en PDB References: 4agr, 4agv, 4agg The structure of a tetrameric sponge galectin suggests a basis for glutamate receptor potentiation. text/html Structure of a tetrameric galectin from Cinachyrella sp. (ball sponge) text http://journals.iucr.org/d/services/forthcoming.html#mh5067 The structures of FtsZ from Staphylococcus aureus (SaFtsZ) in apo, GDP-bound, and PC190723-complex forms are reported, and FtsZ undergoes distinct conformational changes. We discuss these structural features and relate them to the crucial functions of FtsZ. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Takashi Matsui et al. doi: International Union of Crystallography The structures of FtsZ from Staphylococcus aureus (SaFtsZ) in apo, GDP-bound, and PC190723-complex forms are reported, and FtsZ undergoes distinct conformational changes. We discuss these structural features and relate them to the crucial functions of FtsZ. en FTSZ; TUBULIN; CELL DIVISION; CONFORMATIONAL CHANGE; INHIBITOR COMPLEX The structures of FtsZ from Staphylococcus aureus (SaFtsZ) in apo, GDP-bound, and PC190723-complex forms are reported, and FtsZ undergoes distinct conformational changes. We discuss these structural features and relate them to the crucial functions of FtsZ. text/html Structural reorganization of the bacterial cell division protein FtsZ from Staphylococcus aureus text http://journals.iucr.org/d/services/forthcoming.html#dz5248 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Quentin Florence et al. doi: International Union of Crystallography en text/html The crystal structure of Augmenter of Liver Regeneration crystallized in the presence of 50 mM CdCl2 reveals a novel Cd2Cl4O6 cluster that aids in crystal packing text http://journals.iucr.org/d/services/forthcoming.html#pf0087 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Glusker doi:10.1107/S0907444912022342 International Union of Crystallography en BOOK REVIEW text/html Macromolecular Crystallization and Crystal Perfection. By Naomi E. Chayen, John R. Helliwell and Edward H. Snell. Pp. xi + 221. Oxford University Press, 2010. International Union of Crystallography Book Series, Monographs in Crystallography 24. Price (hardback) £65. ISBN: 978-0-19-921325-2. text http://journals.iucr.org/d/services/forthcoming.html#dz5255 Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30-kDa lipoprotein family of mulberry silkworm (Bombyx mori L.) hemolymph have been determined. The hemolymph-isolated protein was identified through successful sequence assignment according to electron density maps at 1.33 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Agnieszka J. Pietrzyk et al. doi: International Union of Crystallography Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30-kDa lipoprotein family of mulberry silkworm (Bombyx mori L.) hemolymph have been determined. The hemolymph-isolated protein was identified through successful sequence assignment according to electron density maps at 1.33 Å resolution. en HEMOLYMPH PROTEIN; 30 KDA LIPOPROTEIN FAMILY; [BETA]-TREFOIL; HEMOLYMPH; SILKWORM; BOMBYX MORI; PROTEIN SEQUENCING Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30-kDa lipoprotein family of mulberry silkworm (Bombyx mori L.) hemolymph have been determined. The hemolymph-isolated protein was identified through successful sequence assignment according to electron density maps at 1.33 Å resolution. text/html High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of protein's identity and potential role in detoxification text http://journals.iucr.org/d/services/forthcoming.html#dz5254 Dose-dependent atomic B-factors are used to determine the average spatial distribution of radiation damage to crystalline thaumatin and urease. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Matthew Warkentin et al. doi: International Union of Crystallography Dose-dependent atomic B-factors are used to determine the average spatial distribution of radiation damage to crystalline thaumatin and urease. en PROTEIN CRYSTALLOGRAPHY; RADIATION DAMAGE; TEMPERATURE DEPENDENCE Dose-dependent atomic B-factors are used to determine the average spatial distribution of radiation damage to crystalline thaumatin and urease. text/html Spatial distribution of radiation damage to crystalline proteins at 25 to 300 K text http://journals.iucr.org/d/services/forthcoming.html#wd5179 The values of atomic shifts in unrestrained refinement can hint alternative conformations. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Sobolev and Lunin doi: International Union of Crystallography The values of atomic shifts in unrestrained refinement can hint alternative conformations. en UNRESTRAINED REFINEMENT; ALTERNATIVE CONFORMATIONS The values of atomic shifts in unrestrained refinement can hint alternative conformations. text/html Detection of alternative conformations by unrestrained refinement text http://journals.iucr.org/d/services/forthcoming.html#cb5010 The 1.0 Å crystal structure of an alternating L-homoalanyl, D-alanyl PNA reveals a novel tetrameric cage with Watson-Crick pairing of the stacked nucleobases. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jose A. Cuesta-Seijo et al. doi: International Union of Crystallography The 1.0 Å crystal structure of an alternating L-homoalanyl, D-alanyl PNA reveals a novel tetrameric cage with Watson-Crick pairing of the stacked nucleobases. en PNA (PEPTIDE NUCLEIC ACID); BASE PAIRING; BASE STACKING; DIRECT METHODS The 1.0 Å crystal structure of an alternating L-homoalanyl, D-alanyl PNA reveals a novel tetrameric cage with Watson-Crick pairing of the stacked nucleobases. text/html Continuous β-Turn Fold of an Alternating Alanyl/Homoalanyl Peptide Nucleic Acid text http://journals.iucr.org/d/services/forthcoming.html#en5495 Structural and functional studies show the importance of palmitic acid transport by the cytosolic protein ReP1-NCXSQ in the regulation of the squid nerve Na+/Ca2+ exchanger NCXSQ1 Abbreviation footnotes: ReP1-NCXSQ, cytosolic regulatory protein of the squid nerve Na+/Ca2+ exchanger; CRABP, cellular retinoic acid binding protein; FABP, fatty acid binding protein, NCX1, mammalian heart Na+/Ca2+ exchanger; NCXSQ1, squid nerve Na+/Ca2+ exchanger; MgATP, Magnesium adenosine 5' triphosphate; LBP, lipid-binding protein; CRBP, cellular retinol binding protein; H+i, intracellular H+; Na+i, intracellular Na+; Ca2+i, intracellular Ca2+; PtdIns(4,5)P2, phosphatidylinositol-4,5 biphosphate; NMG, N-methyl-D-glucamine; CHES, N-Cyclohexyl-2-aminoethanesulfonic acid; MOPS, 3-(N-morpholino)propanesulfonic acid; HRMS, high resolution mass spectrometry; ESI-MS, electrospray ionization mass spectrometry; LC-MS, liquid-chromatography coupled to mass spectrometry. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Alexandra Cousido-Siah et al. doi: International Union of Crystallography Structural and functional studies show the importance of palmitic acid transport by the cytosolic protein ReP1-NCXSQ in the regulation of the squid nerve Na+/Ca2+ exchanger NCXSQ1 Abbreviation footnotes: ReP1-NCXSQ, cytosolic regulatory protein of the squid nerve Na+/Ca2+ exchanger; CRABP, cellular retinoic acid binding protein; FABP, fatty acid binding protein, NCX1, mammalian heart Na+/Ca2+ exchanger; NCXSQ1, squid nerve Na+/Ca2+ exchanger; MgATP, Magnesium adenosine 5' triphosphate; LBP, lipid-binding protein; CRBP, cellular retinol binding protein; H+i, intracellular H+; Na+i, intracellular Na+; Ca2+i, intracellular Ca2+; PtdIns(4,5)P2, phosphatidylinositol-4,5 biphosphate; NMG, N-methyl-D-glucamine; CHES, N-Cyclohexyl-2-aminoethanesulfonic acid; MOPS, 3-(N-morpholino)propanesulfonic acid; HRMS, high resolution mass spectrometry; ESI-MS, electrospray ionization mass spectrometry; LC-MS, liquid-chromatography coupled to mass spectrometry. en FABP PROTEINS; PALMITIC ACID; SQUID NERVE NA+/CA2+ EXCHANGER REGULATION Structural and functional studies show the importance of palmitic acid transport by the cytosolic protein ReP1-NCXSQ in the regulation of the squid nerve Na+/Ca2+ exchanger NCXSQ1 Abbreviation footnotes: ReP1-NCXSQ, cytosolic regulatory protein of the squid nerve Na+/Ca2+ exchanger; CRABP, cellular retinoic acid binding protein; FABP, fatty acid binding protein, NCX1, mammalian heart Na+/Ca2+ exchanger; NCXSQ1, squid nerve Na+/Ca2+ exchanger; MgATP, Magnesium adenosine 5' triphosphate; LBP, lipid-binding protein; CRBP, cellular retinol binding protein; H+i, intracellular H+; Na+i, intracellular Na+; Ca2+i, intracellular Ca2+; PtdIns(4,5)P2, phosphatidylinositol-4,5 biphosphate; NMG, N-methyl-D-glucamine; CHES, N-Cyclohexyl-2-aminoethanesulfonic acid; MOPS, 3-(N-morpholino)propanesulfonic acid; HRMS, high resolution mass spectrometry; ESI-MS, electrospray ionization mass spectrometry; LC-MS, liquid-chromatography coupled to mass spectrometry. text/html STRUCTURAL AND FUNCTIONAL STUDIES OF REP1-NCXSQ, A PROTEIN REGULATING THE SQUID NERVE Na+/Ca2+ EXCHANGER text http://journals.iucr.org/d/services/forthcoming.html#mh5063 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Bellini and Papiz doi: International Union of Crystallography en text/html Dimerization properties of RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesis text http://journals.iucr.org/d/services/forthcoming.html#lv5019 Crystal structures of far-red fluorescent proteins eqFP650 and eqFP670 are solved at 1.8 Å and 1.6 Å resolution, respectively. This permitted identification of the structural elements responsible for bathochromic shift in both considered far-red FPs. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Sergei Pletnev et al. doi: International Union of Crystallography Crystal structures of far-red fluorescent proteins eqFP650 and eqFP670 are solved at 1.8 Å and 1.6 Å resolution, respectively. This permitted identification of the structural elements responsible for bathochromic shift in both considered far-red FPs. en PDB CODES; 4EDO FOR EQFP650; 4EDS FOR EQFP670 FAR-RED FLUORESCENT PROTEINS; CELL IMAGING; TISSUE VISUALIZATION; KATUSHKA Crystal structures of far-red fluorescent proteins eqFP650 and eqFP670 are solved at 1.8 Å and 1.6 Å resolution, respectively. This permitted identification of the structural elements responsible for bathochromic shift in both considered far-red FPs. text/html Structural basis for bathochromic shift of fluorescence in far-red fluorescent proteins eqFP650 and eqFP670 text http://journals.iucr.org/d/services/forthcoming.html#mh5065 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 S. Tishchenko et al. doi: International Union of Crystallography en L1-RNA INTERACTION/CRYSTAL PACKING/L1 STALK/TTHL1 text/html High resolution crystal structure of the isolated ribosomal L1 stalk text http://journals.iucr.org/d/services/forthcoming.html#en5491 Presented is the first X-ray structure of p38α co-crystallized with TAK-715, as well as new high resolution structures of p38α bound to SB-203580, SCIO-469, and VX-745. The impact of crystallization conditions and selectivity profiles on protein conformation is discussed. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Rita Azevedo et al. doi: International Union of Crystallography Presented is the first X-ray structure of p38α co-crystallized with TAK-715, as well as new high resolution structures of p38α bound to SB-203580, SCIO-469, and VX-745. The impact of crystallization conditions and selectivity profiles on protein conformation is discussed. en P38[ALPHA]; TAK-715; SB-203580; SCIO-469; VX-745; SELECTIVITY; SOAKING; PROTEIN KINASE; INHIBITOR DESIGN Presented is the first X-ray structure of p38α co-crystallized with TAK-715, as well as new high resolution structures of p38α bound to SB-203580, SCIO-469, and VX-745. The impact of crystallization conditions and selectivity profiles on protein conformation is discussed. text/html X-ray structure of p38α bound to TAK-715: Comparison to three classic inhibitors text http://journals.iucr.org/d/services/forthcoming.html#rr5019 The crystal structure of MoSub1, Sub1/PC4 ortholog from rice blast fungus, has two novel features in the N-terminal and C-terminal to the DNA binding domain. It has similar dimer interface and DNA binding region to PC4 and the protein binds single stranded DNA tightly. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jinguang Huang et al. doi: International Union of Crystallography The crystal structure of MoSub1, Sub1/PC4 ortholog from rice blast fungus, has two novel features in the N-terminal and C-terminal to the DNA binding domain. It has similar dimer interface and DNA binding region to PC4 and the protein binds single stranded DNA tightly. en MOSUB1; MAGNAPORTHE ORYZAE; SUB1/PC4; SSDNA BINDING PROTEIN The crystal structure of MoSub1, Sub1/PC4 ortholog from rice blast fungus, has two novel features in the N-terminal and C-terminal to the DNA binding domain. It has similar dimer interface and DNA binding region to PC4 and the protein binds single stranded DNA tightly. text/html Structure features of single strand DNA(ssDNA) binding protein MoSub1 from Magnaporthe oryzae text http://journals.iucr.org/d/services/forthcoming.html#cb5008 Glucosamine-6-phosphate N-acetyltransferase is an essential enzyme of the eukaryotic UDP-GlcNAc biosynthetic pathway. A crystal structure at 1.55 Å resolution reveals a highly unusual covalent product complex and biochemical studies investigate the function of a fully conserved active site cysteine. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Helge C. Dorfmueller et al. doi: International Union of Crystallography Glucosamine-6-phosphate N-acetyltransferase is an essential enzyme of the eukaryotic UDP-GlcNAc biosynthetic pathway. A crystal structure at 1.55 Å resolution reveals a highly unusual covalent product complex and biochemical studies investigate the function of a fully conserved active site cysteine. en CARBOHYDRATE; GLYCOBIOLOGY; STRUCTURE; C.ELEGANS; GLUCOSAMINE-6-PHOSPHATE N-ACETYLTRANSFERASE; COENZYME A ADDUCT; MECHANISM Glucosamine-6-phosphate N-acetyltransferase is an essential enzyme of the eukaryotic UDP-GlcNAc biosynthetic pathway. A crystal structure at 1.55 Å resolution reveals a highly unusual covalent product complex and biochemical studies investigate the function of a fully conserved active site cysteine. text/html Structural and biochemical characterization of a trapped coenzyme A adduct of C. elegans glucosamine-6-phosphate N-acetyltransferase text http://journals.iucr.org/d/services/forthcoming.html#mh5062 The promiscuous binding of a NS5A peptide to the Fyn-SH3 domain Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jose Manuel Martin-Garcia et al. doi: International Union of Crystallography The promiscuous binding of a NS5A peptide to the Fyn-SH3 domain en SH3 DOMAIN; X-RAY STRUCTURE; FYN TYROSINE KINASE; NS5A; HEPATITIS C VIRUS; PROLINE RICH MOTIFS The promiscuous binding of a NS5A peptide to the Fyn-SH3 domain text/html The promiscuous binding of the Fyn-SH3 domain to a peptide from the NS5A protein text http://journals.iucr.org/d/services/forthcoming.html#dw5018 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Travis A. Pemberton et al. doi: International Union of Crystallography en text/html Proline: Mother Nature's Cryoprotectant Applied to Protein Crystallography text http://journals.iucr.org/d/services/forthcoming.html#be5201 A rapid, plate-based pH assay has been developed that takes advantage of automation available in a protein crystallization laboratory. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Newman, Sayle and Fazio doi: International Union of Crystallography A rapid, plate-based pH assay has been developed that takes advantage of automation available in a protein crystallization laboratory. en UNIVERSAL INDICATOR; PH ASSAY; HIGH THROUGHPUT A rapid, plate-based pH assay has been developed that takes advantage of automation available in a protein crystallization laboratory. text/html A universal indicator dye pH assay for crystallization solutions and other high-throughput applications text http://journals.iucr.org/d/services/forthcoming.html#gm5021 A powerful and easy to use workflow environment has been developed at the ESRF for combining experiment control with on-line data analysis on synchrotron beamlines. This tool opens the possibility of automating complex experiments without the need of expertise in instrumentation control and programming, but rather accessing defined beamline services. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Sandor Brockhauser et al. doi: International Union of Crystallography A powerful and easy to use workflow environment has been developed at the ESRF for combining experiment control with on-line data analysis on synchrotron beamlines. This tool opens the possibility of automating complex experiments without the need of expertise in instrumentation control and programming, but rather accessing defined beamline services. en WORKFLOW; AUTOMATION; DATA PROCESSING; MACROMOLECULAR CRYSTALLOGRAPHY; EXPERIMENTAL PROTOCOL; CHARACTERIZATION; REORIENTATION; RADIATION DAMAGE A powerful and easy to use workflow environment has been developed at the ESRF for combining experiment control with on-line data analysis on synchrotron beamlines. This tool opens the possibility of automating complex experiments without the need of expertise in instrumentation control and programming, but rather accessing defined beamline services. text/html The Use of Workflows in the Design and Implementation of Complex Experiments in Macromolecular Crystallography text http://journals.iucr.org/d/services/forthcoming.html#rr5014 RCrane is a new tool for the partially automated building of RNA crystallographic models into electron density maps of low or intermediate resolution. This tool helps crystallographers to place phosphates and bases into electron density, and then automatically predicts and builds the detailed all-atom structure of the traced nucleotides. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Keating and Pyle doi: International Union of Crystallography RCrane is a new tool for the partially automated building of RNA crystallographic models into electron density maps of low or intermediate resolution. This tool helps crystallographers to place phosphates and bases into electron density, and then automatically predicts and builds the detailed all-atom structure of the traced nucleotides. en RCrane is a new tool for the partially automated building of RNA crystallographic models into electron density maps of low or intermediate resolution. This tool helps crystallographers to place phosphates and bases into electron density, and then automatically predicts and builds the detailed all-atom structure of the traced nucleotides. text/html RCrane: Semi-automated RNA model building text http://journals.iucr.org/d/services/forthcoming.html#xb5055 We report the crystal structure of the branched-chain aminotransferase from Streptococcus mutans to 1.9 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jing Ruan et al. doi: International Union of Crystallography We report the crystal structure of the branched-chain aminotransferase from Streptococcus mutans to 1.9 Å resolution. en STREPTOCOCCUS MUTANS; SMILVE We report the crystal structure of the branched-chain aminotransferase from Streptococcus mutans to 1.9 Å resolution. text/html Structure of the branched-chain aminotransferase from Streptococcus mutans text http://journals.iucr.org/d/services/forthcoming.html#mv5064 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Amit Sharma et al. doi: International Union of Crystallography en DNA POLYMERASE; Y-FAMILY; ENZYME STRUCTURE; MOLECULAR BIOLOGY; MUTAGENESIS; MYCOBACTERIA; PAD REGION text/html The PAD region in the mycobacterial dinB homolog MsPolIV exhibits positional heterogeneity text http://journals.iucr.org/d/services/forthcoming.html#rr5017 All-atom models derived from moderate-resolution protein crystal structures contain a high frequency of close nonbonded contacts, independent of the major refinement program used for structure determination. All-atom refinement with PrimeX corrects many of these problematic interactions, producing models that are better suited for use in computational chemistry and related applications. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Bell et al. doi: International Union of Crystallography All-atom models derived from moderate-resolution protein crystal structures contain a high frequency of close nonbonded contacts, independent of the major refinement program used for structure determination. All-atom refinement with PrimeX corrects many of these problematic interactions, producing models that are better suited for use in computational chemistry and related applications. en H ATOMS; VAN DER WAALS RADII; RESTRAINTS; NONBONDED CONTACTS; CLASHES; MOLECULAR GEOMETRY; MODEL QUALITY; FORCE FIELD; REFINEMENT; RIDING H ATOMS; ELECTROSTATICS; HYDROGEN BONDS All-atom models derived from moderate-resolution protein crystal structures contain a high frequency of close nonbonded contacts, independent of the major refinement program used for structure determination. All-atom refinement with PrimeX corrects many of these problematic interactions, producing models that are better suited for use in computational chemistry and related applications. text/html Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX text http://journals.iucr.org/d/services/forthcoming.html#rr5008 The crystal structures of YrdA from E. coli show conformations that have not been reported in γ-class carbonic anhydrase family proteins. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Park et al. doi:10.1107/S0907444912017210 International Union of Crystallography The crystal structures of YrdA from E. coli show conformations that have not been reported in γ-class carbonic anhydrase family proteins. en YRDA; [GAMMA]-CLASS CARBONIC ANHYDRASES The crystal structures of YrdA from E. coli show conformations that have not been reported in γ-class carbonic anhydrase family proteins. text/html Structures of the γ-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch text http://journals.iucr.org/d/services/forthcoming.html#xb5051 The structure of ustiloxin D bound to tubulin was determined at a resolution which allows interatomic interactions to be defined and provides a basis for the structure-based design of ligands with improved activity. It is also shown how local interactions of vinca-domain ligands with tubulin influence the relative positioning of the latter and lead to the large-scale polymorphism of ligand-mediated tubulin assemblies. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Ranaivoson et al. doi:10.1107/S0907444912017143 International Union of Crystallography The structure of ustiloxin D bound to tubulin was determined at a resolution which allows interatomic interactions to be defined and provides a basis for the structure-based design of ligands with improved activity. It is also shown how local interactions of vinca-domain ligands with tubulin influence the relative positioning of the latter and lead to the large-scale polymorphism of ligand-mediated tubulin assemblies. en MICROTUBULES; PHOMOPSIN A; PROTOFILAMENTS; USTILOXIN; VINBLASTINE The structure of ustiloxin D bound to tubulin was determined at a resolution which allows interatomic interactions to be defined and provides a basis for the structure-based design of ligands with improved activity. It is also shown how local interactions of vinca-domain ligands with tubulin influence the relative positioning of the latter and lead to the large-scale polymorphism of ligand-mediated tubulin assemblies. text/html Structural plasticity of tubulin assembly probed by vinca-domain ligands text http://journals.iucr.org/d/services/forthcoming.html#cb5005 The three-dimensional structure of an industrially relevant cellulase in complex with ligands has been determined at a resolution of 1.9 Å. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Thompson et al. doi:10.1107/S0907444912016496 International Union of Crystallography The three-dimensional structure of an industrially relevant cellulase in complex with ligands has been determined at a resolution of 1.9 Å. en CELLULASES; BIOETHANOL; CELLOBIOHYDROLASES; CELLULOSE; CELLOBIOSE The three-dimensional structure of an industrially relevant cellulase in complex with ligands has been determined at a resolution of 1.9 Å. text/html The structure of the catalytic core module of the Chaetomium thermophilum family GH6 cellobiohydrolase Cel6A text http://journals.iucr.org/d/services/forthcoming.html#rr5013 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Klopffleisch et al. doi:10.1107/S0907444912016587 International Union of Crystallography en PROTEIN KINASE CK2; CASEIN KINASE 2; RESORUFIN; HINGE-REGION PLASTICITY; LYOTROPIC SALTS text/html Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: a tool to study the unique hinge-region plasticity of the enzyme without packing bias text http://journals.iucr.org/d/services/forthcoming.html#nj5116 Acoustic droplet ejection achieves precise, tipless, non-invasive transfer of diverse aqueous solutions, enabling nanolitre-scale crystallization trials. The rapid and scalable technique demonstrated successful crystal growth with diverse targets in drop volumes as small as 20 nl. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Villaseñor et al. doi:10.1107/S0907444912016617 International Union of Crystallography Acoustic droplet ejection achieves precise, tipless, non-invasive transfer of diverse aqueous solutions, enabling nanolitre-scale crystallization trials. The rapid and scalable technique demonstrated successful crystal growth with diverse targets in drop volumes as small as 20 nl. en ACOUSTIC LIQUID TRANSFER; NANOLITRE-SCALE CRYSTALLIZATION Acoustic droplet ejection achieves precise, tipless, non-invasive transfer of diverse aqueous solutions, enabling nanolitre-scale crystallization trials. The rapid and scalable technique demonstrated successful crystal growth with diverse targets in drop volumes as small as 20 nl. text/html Nanolitre-scale crystallization using acoustic liquid-transfer technology text http://journals.iucr.org/d/services/forthcoming.html#mh5059 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Zeth et al. doi:10.1107/S0907444912016447 International Union of Crystallography en PII PROTEINS; SYNECHOCOCCUS ELONGATUS text/html An engineered PII protein variant that senses a novel ligand: atomic resolution structure of the complex with citrate text http://journals.iucr.org/d/services/forthcoming.html#mv5063 O-Acetylserine sulfhydrylase (OASS) from L. donovani can bind to serine acetyltransferase (SAT) C-terminus mimicking peptides with a range of bulkiness; the strength of these interactions correlates with the size of the peptide side chains and the size of the active-site cleft. Differences in the interactions of OASS and SAT from various species may be explained by the size of the active-site cleft. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Raj et al. doi:10.1107/S0907444912016459 International Union of Crystallography O-Acetylserine sulfhydrylase (OASS) from L. donovani can bind to serine acetyltransferase (SAT) C-terminus mimicking peptides with a range of bulkiness; the strength of these interactions correlates with the size of the peptide side chains and the size of the active-site cleft. Differences in the interactions of OASS and SAT from various species may be explained by the size of the active-site cleft. en CYSTEINE-BIOSYNTHETIC PATHWAY; CYSTEINE SYNTHASE COMPLEX; SAT C-TERMINUS MIMICKING PEPTIDES; REGULATION; INHIBITION O-Acetylserine sulfhydrylase (OASS) from L. donovani can bind to serine acetyltransferase (SAT) C-terminus mimicking peptides with a range of bulkiness; the strength of these interactions correlates with the size of the peptide side chains and the size of the active-site cleft. Differences in the interactions of OASS and SAT from various species may be explained by the size of the active-site cleft. text/html The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences text http://journals.iucr.org/d/services/forthcoming.html#kw5044 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Terwilliger et al. doi:10.1107/S0907444912015636 International Union of Crystallography en MOLECULAR REPLACEMENT; AUTOMATION; MACROMOLECULAR CRYSTALLOGRAPHY; STRUCTURE SIMILARITY; MODELING; PHENIX; MORPHING text/html Improved crystallographic models through iterated local density-guided model deformation and reciprocal-space refinement text http://journals.iucr.org/d/services/forthcoming.html#mn5009 ATP bound in the active site of protein kinase A is readily hydrolysed to ADP and free phosphate by X-ray irradiation at room temperature. The phosphate ion observed in the active site causes a dramatic conformational change of the bound peptide inhibitor. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Kovalevsky et al. doi:10.1107/S0907444912014886 International Union of Crystallography ATP bound in the active site of protein kinase A is readily hydrolysed to ADP and free phosphate by X-ray irradiation at room temperature. The phosphate ion observed in the active site causes a dramatic conformational change of the bound peptide inhibitor. en PROTEIN KINASE A; ATPASES; ATP HYDROLYSIS ATP bound in the active site of protein kinase A is readily hydrolysed to ADP and free phosphate by X-ray irradiation at room temperature. The phosphate ion observed in the active site causes a dramatic conformational change of the bound peptide inhibitor. text/html Low- and room-temperature X-ray structures of protein kinase A ternary complexes shed new light on its activity text http://journals.iucr.org/d/services/forthcoming.html#lv5018 The crystal structure of a putative general stress protein from the citrus canker bacterium X. citri pv. citri was determined to 2.5 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Hilario et al. doi:10.1107/S0907444912014126 International Union of Crystallography The crystal structure of a putative general stress protein from the citrus canker bacterium X. citri pv. citri was determined to 2.5 Å resolution. en CITRUS CANKER; GENERAL STRESS PROTEINS; XANTHOMONAS CITRI PV. CITRI; XAC2369 GENE; XACGSP; OXIDATIVE STRESS The crystal structure of a putative general stress protein from the citrus canker bacterium X. citri pv. citri was determined to 2.5 Å resolution. text/html The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding property text http://journals.iucr.org/d/services/forthcoming.html#rr5011 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Celikel et al. doi:10.1107/S090744491201373X International Union of Crystallography en HISTIDINE KINASES; ATP-BINDING DOMAINS; INTACT ATP text/html ATP forms a stable complex with the essential histidine kinase WalK (YycG) domain text http://journals.iucr.org/d/services/forthcoming.html#gm5020 Crystal structures of the family 3b carbohydrate-binding module (CBM3b) of the cellulosomal multimodular hydrolytic enzyme cellobiohydrolase 9A (Cbh9A) from C. thermocellum and of its mutant Cbh9A CBM3bN126W have been determined at 2.20 and 1.04 Å resolution, respectively. This mutation restores the cellulose-binding properties of the adhesion-deficient CBM. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Yaniv et al. doi:10.1107/S0907444912013133 International Union of Crystallography Crystal structures of the family 3b carbohydrate-binding module (CBM3b) of the cellulosomal multimodular hydrolytic enzyme cellobiohydrolase 9A (Cbh9A) from C. thermocellum and of its mutant Cbh9A CBM3bN126W have been determined at 2.20 and 1.04 Å resolution, respectively. This mutation restores the cellulose-binding properties of the adhesion-deficient CBM. en FAMILY 3 CARBOHYDRATE-BINDING MODULES; CELLOBIOHYDROLASE 9A; CLOSTRIDIUM THERMOCELLUM Crystal structures of the family 3b carbohydrate-binding module (CBM3b) of the cellulosomal multimodular hydrolytic enzyme cellobiohydrolase 9A (Cbh9A) from C. thermocellum and of its mutant Cbh9A CBM3bN126W have been determined at 2.20 and 1.04 Å resolution, respectively. This mutation restores the cellulose-binding properties of the adhesion-deficient CBM. text/html A single mutation restores the binding activity of an adhesion-deficient family 3 carbohydrate-binding module text http://journals.iucr.org/d/services/forthcoming.html#mh5058 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jeng et al. doi:10.1107/S0907444912013224 International Union of Crystallography en OLIGOSACCHARIDE SYNTHESIS; TRANSGLYCOSYLATION; NKBGL; NEOTERMES KOSHUNENSIS; GLYCOSYL HYDROLASE FAMILY 1; [BETA]-GLUCOSIDASES text/html High-resolution structures of Neotermes koshunensis β-glucosidase mutants provide insights into the catalytic mechanism and the synthesis of glucoconjugates text http://journals.iucr.org/d/services/forthcoming.html#yt5040 A bond-distance analysis to determine the protonation states of ionizable amino acids has been made for trypsin at 1.2 Å resolution, subtilisin at 1.26 Å resolution and lysozyme at 0.65 Å resolution. This was effective for Asp and Glu but not for His. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Fisher et al. doi:10.1107/S0907444912012589 International Union of Crystallography A bond-distance analysis to determine the protonation states of ionizable amino acids has been made for trypsin at 1.2 Å resolution, subtilisin at 1.26 Å resolution and lysozyme at 0.65 Å resolution. This was effective for Asp and Glu but not for His. en PROTONATION STATES; IONIZABLE AMINO ACIDS; BOND-DISTANCE ANALYSIS A bond-distance analysis to determine the protonation states of ionizable amino acids has been made for trypsin at 1.2 Å resolution, subtilisin at 1.26 Å resolution and lysozyme at 0.65 Å resolution. This was effective for Asp and Glu but not for His. text/html Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness text http://journals.iucr.org/d/services/forthcoming.html#tz5006 A systematic increase in lifetime is observed in room-temperature protein and virus crystals through the use of reduced exposure times and a fast detector. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Owen et al. doi:10.1107/S0907444912012553 International Union of Crystallography A systematic increase in lifetime is observed in room-temperature protein and virus crystals through the use of reduced exposure times and a fast detector. en RADIATION DAMAGE; ROOM TEMPERATURE; DOSE RATE; FREE RADICALS A systematic increase in lifetime is observed in room-temperature protein and virus crystals through the use of reduced exposure times and a fast detector. text/html Outrunning free radicals in room-temperature macromolecular crystallography text http://journals.iucr.org/d/services/forthcoming.html#mv5058 The structure of potato serine protease inhibitor, the most abundant protease inhibitor in potatoes, is reported and sheds light on the inhibition mechanism of this protein. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Meulenbroek et al. doi:10.1107/S090744491201222X International Union of Crystallography The structure of potato serine protease inhibitor, the most abundant protease inhibitor in potatoes, is reported and sheds light on the inhibition mechanism of this protein. en KUNITZ-TYPE SERINE PROTEASE INHIBITORS; POTATO The structure of potato serine protease inhibitor, the most abundant protease inhibitor in potatoes, is reported and sheds light on the inhibition mechanism of this protein. text/html Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato text http://journals.iucr.org/d/services/forthcoming.html#wd5173 A 16 Å resolution molecular envelope of Na+-translocating NADH:ubiquinone oxidoreductase was determined by connectivity-based ab initio phasing. The low-resolution structure of this multi-subunit membrane complex was confirmed by negative-stain electron microscopy. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Lunin et al. doi:10.1107/S0907444912012012 International Union of Crystallography A 16 Å resolution molecular envelope of Na+-translocating NADH:ubiquinone oxidoreductase was determined by connectivity-based ab initio phasing. The low-resolution structure of this multi-subunit membrane complex was confirmed by negative-stain electron microscopy. en NA+-TRANSLOCATING NADH:UBIQUINONE OXIDOREDUCTASE; MEMBRANE PROTEINS; LOW RESOLUTION; AB INITIO PHASING A 16 Å resolution molecular envelope of Na+-translocating NADH:ubiquinone oxidoreductase was determined by connectivity-based ab initio phasing. The low-resolution structure of this multi-subunit membrane complex was confirmed by negative-stain electron microscopy. text/html Low-resolution structure determination of Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy text http://journals.iucr.org/d/services/forthcoming.html#be5200 This article presents a set of preliminary publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution, and discusses the rationale for their application. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Jacques et al. doi:10.1107/S0907444912012073 International Union of Crystallography This article presents a set of preliminary publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution, and discusses the rationale for their application. en SMALL-ANGLE SCATTERING; PUBLICATION GUIDELINES This article presents a set of preliminary publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution, and discusses the rationale for their application. text/html Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution text http://journals.iucr.org/d/services/forthcoming.html#mh5056 Crystal structures of peptide deformylase from S. aureus in complex with novel inhibitors are presented together with their functional analysis. A detailed comparative analysis of these structures as well as the activities of the inhibitors allowed the elucidation of distinctive structural changes which depend upon the class of inhibitor. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Lee et al. doi:10.1107/S0907444912011912 International Union of Crystallography Crystal structures of peptide deformylase from S. aureus in complex with novel inhibitors are presented together with their functional analysis. A detailed comparative analysis of these structures as well as the activities of the inhibitors allowed the elucidation of distinctive structural changes which depend upon the class of inhibitor. en ANTIMICROBIAL AGENTS; PDF; PEPTIDE DEFORMYLASES; STAPHYLOCOCCUS AUREUS Crystal structures of peptide deformylase from S. aureus in complex with novel inhibitors are presented together with their functional analysis. A detailed comparative analysis of these structures as well as the activities of the inhibitors allowed the elucidation of distinctive structural changes which depend upon the class of inhibitor. text/html Structures of Staphylococcus aureus peptide deformylase in complex with two classes of new inhibitors text http://journals.iucr.org/d/services/forthcoming.html#en5489 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Chu et al. doi:10.1107/S0907444912011407 International Union of Crystallography en URIDYLATE KINASE; HELICOBACTER PYLORI text/html Structures of Helicobacter pylori uridylate kinase: insight into release of the product UDP text http://journals.iucr.org/d/services/forthcoming.html#dz5252 The distribution of twinned intensities may be biased towards the Wilson distribution if a noncrystallographic screw axis parallel to the twinning axis is present. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Lunin doi:10.1107/S0907444912011420 International Union of Crystallography The distribution of twinned intensities may be biased towards the Wilson distribution if a noncrystallographic screw axis parallel to the twinning axis is present. en HEMIHEDRAL TWINNING; INTENSITY STATISTICS; NONCRYSTALLOGRAPHIC SYMMETRY The distribution of twinned intensities may be biased towards the Wilson distribution if a noncrystallographic screw axis parallel to the twinning axis is present. text/html A noncrystallographic screw axis parallel to a twin axis can corrupt intensity statistics text http://journals.iucr.org/d/services/forthcoming.html#dz5250 X-ray structures of S. solfataricus serine:pyruvate aminotransferase in different intermediate states and in complex with inhibitor have increased our understanding of the enzyme mechanism and have allowed an insight into the substrate specificity of this industrially important enzyme. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Sayer et al. doi:10.1107/S0907444912011274 International Union of Crystallography X-ray structures of S. solfataricus serine:pyruvate aminotransferase in different intermediate states and in complex with inhibitor have increased our understanding of the enzyme mechanism and have allowed an insight into the substrate specificity of this industrially important enzyme. en PYRIDOXAL 5'-PHOSPHATE; TRANSAMINASES; GABACULINE; SUBSTRATE SPECIFICITY X-ray structures of S. solfataricus serine:pyruvate aminotransferase in different intermediate states and in complex with inhibitor have increased our understanding of the enzyme mechanism and have allowed an insight into the substrate specificity of this industrially important enzyme. text/html Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus text http://journals.iucr.org/d/services/forthcoming.html#dw5013 Succinyl-CoA synthetase catalyzes the reaction succinyl-CoA + NDP + Pi ⇌ succinate + CoA + NTP, where N denotes adenosine or guanosine. The enzyme from T. aquaticus was characterized biochemically and its structure was determined in complex with GDP-Mn2+, the preferred nucleotide. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Joyce et al. doi:10.1107/S0907444912010852 International Union of Crystallography Succinyl-CoA synthetase catalyzes the reaction succinyl-CoA + NDP + Pi ⇌ succinate + CoA + NTP, where N denotes adenosine or guanosine. The enzyme from T. aquaticus was characterized biochemically and its structure was determined in complex with GDP-Mn2+, the preferred nucleotide. en THERMOSTABILITY; DENATURATION; NUCLEOTIDE SPECIFICITY; ATP-GRASP FOLD; ENZYME KINETICS Succinyl-CoA synthetase catalyzes the reaction succinyl-CoA + NDP + Pi ⇌ succinate + CoA + NTP, where N denotes adenosine or guanosine. The enzyme from T. aquaticus was characterized biochemically and its structure was determined in complex with GDP-Mn2+, the preferred nucleotide. text/html Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus text http://journals.iucr.org/d/services/forthcoming.html#mv5059 Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 de Barros et al. doi:10.1107/S0907444912010281 International Union of Crystallography en IMPORTIN [ALPHA]; NUCLEAR IMPORT PATHWAY; NUCLEAR LOCALIZATION SEQUENCE; DNA-REPAIR PROTEINS; FEN1 text/html Structural basis of nuclear import of flap endonuclease 1 (FEN1) text http://journals.iucr.org/d/services/forthcoming.html#kw5042 1.40 and 1.26 Å resolution crystal structures of potato endo-1,3-β-glucanase, a member of glycoside hydrolase family 17, reveal high flexibility of a subdomain that forms part of the active-site cleft and an unusual crystal-packing mode characterized by infinite chains of protein molecules linked via His-tag docking in the next active site. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Wojtkowiak et al. doi:10.1107/S090744491200995X International Union of Crystallography 1.40 and 1.26 Å resolution crystal structures of potato endo-1,3-β-glucanase, a member of glycoside hydrolase family 17, reveal high flexibility of a subdomain that forms part of the active-site cleft and an unusual crystal-packing mode characterized by infinite chains of protein molecules linked via His-tag docking in the next active site. en GLYCOSIDE HYDROLASES; GH17; SUBDOMAINS; PATHOGENESIS-RELATED PROTEINS; HIS TAGS; CRYSTAL PACKING 1.40 and 1.26 Å resolution crystal structures of potato endo-1,3-β-glucanase, a member of glycoside hydrolase family 17, reveal high flexibility of a subdomain that forms part of the active-site cleft and an unusual crystal-packing mode characterized by infinite chains of protein molecules linked via His-tag docking in the next active site. text/html Two high-resolution structures of potato endo-1,3-β-glucanase reveal subdomain flexibility with implications for substrate binding text http://journals.iucr.org/d/services/forthcoming.html#hv5206 D. radiodurans AlkA consists of only two domains instead of three as for E. coli AlkA. This structural modification alters the substrate specificity which may contribute to an improved DNA-repair repertoire of this extreme radiation resistant organism. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Moe et al. doi:10.1107/S090744491200947X International Union of Crystallography D. radiodurans AlkA consists of only two domains instead of three as for E. coli AlkA. This structural modification alters the substrate specificity which may contribute to an improved DNA-repair repertoire of this extreme radiation resistant organism. en 3-METHYLADENINE DNA GLYCOSYLASE II; ALKA; DNA-REPAIR ENZYMES; DEINOCOCCUS RADIODURANS D. radiodurans AlkA consists of only two domains instead of three as for E. coli AlkA. This structural modification alters the substrate specificity which may contribute to an improved DNA-repair repertoire of this extreme radiation resistant organism. text/html Structure–function studies of an unusual 3-methyladenine DNA glycosylase II (AlkA) from Deinococcus radiodurans text http://journals.iucr.org/d/services/forthcoming.html#rr5016 Crystal structures of factor XIIa inhibitor infestin 4 and infestin 1–trypsin complex have been refined at 1.4 and 2.5 Å resolutions, respectively. Mutants of infestin 4 highly specific to factor XIIa were selected by phage display. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Campos et al. doi:10.1107/S0907444912009067 International Union of Crystallography Crystal structures of factor XIIa inhibitor infestin 4 and infestin 1–trypsin complex have been refined at 1.4 and 2.5 Å resolutions, respectively. Mutants of infestin 4 highly specific to factor XIIa were selected by phage display. en TRIATOMA INFESTANS; KAZAL-TYPE SERINE PROTEASE INHIBITORS; BLOOD COAGULATION; THROMBIN INHIBITORS; FACTOR XIIA INHIBITORS Crystal structures of factor XIIa inhibitor infestin 4 and infestin 1–trypsin complex have been refined at 1.4 and 2.5 Å resolutions, respectively. Mutants of infestin 4 highly specific to factor XIIa were selected by phage display. text/html The Kazal-type inhibitors infestins 1 and 4 differ in specificity but are similar in three-dimensional structure text http://journals.iucr.org/d/services/forthcoming.html#mv5061 The crystal structure of ShSPI, a serpin from the blood fluke S. haematobium, reveals some peculiar features of the helical subdomain which have not been observed previously in the serpin superfamily. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Granzin et al. doi:10.1107/S0907444912008372 International Union of Crystallography The crystal structure of ShSPI, a serpin from the blood fluke S. haematobium, reveals some peculiar features of the helical subdomain which have not been observed previously in the serpin superfamily. en SERPINS; SCHISTOSOMA HAEMATOBIUM; PROTEASE INHIBITORS; PARASITES The crystal structure of ShSPI, a serpin from the blood fluke S. haematobium, reveals some peculiar features of the helical subdomain which have not been observed previously in the serpin superfamily. text/html Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain text http://journals.iucr.org/d/services/forthcoming.html#xb5047 The crystal structure of human RSK1 C-terminal kinase domain (CTKD) is reported at 2.7 Å resolution. The structure indicates that the autoinhibition of the CTKD is caused by an α-helix occupying the substrate-binding groove. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Li et al. doi:10.1107/S0907444912007457 International Union of Crystallography The crystal structure of human RSK1 C-terminal kinase domain (CTKD) is reported at 2.7 Å resolution. The structure indicates that the autoinhibition of the CTKD is caused by an α-helix occupying the substrate-binding groove. en RSK1; CANCER; P90 RIBOSOMAL S6 KINASE; AUTOINHIBITION The crystal structure of human RSK1 C-terminal kinase domain (CTKD) is reported at 2.7 Å resolution. The structure indicates that the autoinhibition of the CTKD is caused by an α-helix occupying the substrate-binding groove. text/html Structural basis for the autoinhibition of the C-­terminal kinase domain of human RSK1 text http://journals.iucr.org/d/services/forthcoming.html#mv5055 Crystal structures of aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis in complex with glycerol and with cysteine are presented. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Vyas et al. doi:10.1107/S0907444912007330 International Union of Crystallography Crystal structures of aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis in complex with glycerol and with cysteine are presented. en ASADH; ASA; ESSENTIAL GENES; ANTIMICROBIAL TARGETS; SMCS Crystal structures of aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis in complex with glycerol and with cysteine are presented. text/html Structures of ternary complexes of aspartate-semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv text http://journals.iucr.org/d/services/forthcoming.html#rr5015 The crystal structure and biochemical properties of the C-terminal catalytic domain of SSV1 integrase, an archaeal member of the tyrosine recombinase family, are described. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Zhan et al. doi:10.1107/S0907444912007202 International Union of Crystallography The crystal structure and biochemical properties of the C-terminal catalytic domain of SSV1 integrase, an archaeal member of the tyrosine recombinase family, are described. en CATALYTIC DOMAINS; INTEGRASE; SSV1; ARCHAEA The crystal structure and biochemical properties of the C-terminal catalytic domain of SSV1 integrase, an archaeal member of the tyrosine recombinase family, are described. text/html Structural and functional characterization of the C-­terminal catalytic domain of SSV1 integrase text http://journals.iucr.org/d/services/forthcoming.html#rr5012 The structure of a xylanase from F. oxysporum (FoXyn10a) was determined at 1.94 Å resolution. FoXyn10a adopts the (α/β)8-barrel fold of the GH10 family, with an extended loop above the catalytic site with potential implications for enzymatic function. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Dimarogona et al. doi:10.1107/S0907444912007044 International Union of Crystallography The structure of a xylanase from F. oxysporum (FoXyn10a) was determined at 1.94 Å resolution. FoXyn10a adopts the (α/β)8-barrel fold of the GH10 family, with an extended loop above the catalytic site with potential implications for enzymatic function. en GH10 XYLANASES; FUSARIUM OXYSPORUM; BIOCATALYSTS The structure of a xylanase from F. oxysporum (FoXyn10a) was determined at 1.94 Å resolution. FoXyn10a adopts the (α/β)8-barrel fold of the GH10 family, with an extended loop above the catalytic site with potential implications for enzymatic function. text/html The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft text http://journals.iucr.org/d/services/forthcoming.html#lv5017 Much more accurate anomalous signal and greater success in substructure determination can be obtained by merging data from multiple crystals preselected according to the results of cluster analysis. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Giordano et al. doi:10.1107/S0907444912006841 International Union of Crystallography Much more accurate anomalous signal and greater success in substructure determination can be obtained by merging data from multiple crystals preselected according to the results of cluster analysis. en MULTIPLE-CRYSTAL DATA COLLECTION; CLUSTERING Much more accurate anomalous signal and greater success in substructure determination can be obtained by merging data from multiple crystals preselected according to the results of cluster analysis. text/html The application of hierarchical cluster analysis to the selection of isomorphous crystals text http://journals.iucr.org/d/services/forthcoming.html#mv5053 The structures of formylglycinamide ribonucleotide amidotransferase from S. typhimurium either with an unliganded glutaminase domain or in complex with an ATP analogue revealed that no major conformational changes take place upon formation of the glutamyl thioester intermediate or subsequent ATP complexation; therefore, formylglycinamide ribonucleotide binding is proposed to be the mechanism of activation of catalytic coupling in the enzyme. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Tanwar et al. doi:10.1107/S0907444912006543 International Union of Crystallography The structures of formylglycinamide ribonucleotide amidotransferase from S. typhimurium either with an unliganded glutaminase domain or in complex with an ATP analogue revealed that no major conformational changes take place upon formation of the glutamyl thioester intermediate or subsequent ATP complexation; therefore, formylglycinamide ribonucleotide binding is proposed to be the mechanism of activation of catalytic coupling in the enzyme. en AMIDOTRANSFERASES; CATALYTIC COUPLING; GLUTAMINASES; THIOESTER INTERMEDIATE; PURINE BIOSYNTHESIS The structures of formylglycinamide ribonucleotide amidotransferase from S. typhimurium either with an unliganded glutaminase domain or in complex with an ATP analogue revealed that no major conformational changes take place upon formation of the glutamyl thioester intermediate or subsequent ATP complexation; therefore, formylglycinamide ribonucleotide binding is proposed to be the mechanism of activation of catalytic coupling in the enzyme. text/html Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling text http://journals.iucr.org/d/services/forthcoming.html#cb5007 Fam96a is a mammalian DUF59 protein, but its structure diverges from those of bacterial DUF59 proteins. Structural clues suggest similarities between Fam96a and amyloidogenic proteins. Copyright (c) 2012 International Union of Crystallography urn:issn:0907-4449 Chen et al. doi:10.1107/S0907444912006592 International Union of Crystallography Fam96a is a mammalian DUF59 protein, but its structure diverges from those of bacterial DUF59 proteins. Structural clues suggest similarities between Fam96a and amyloidogenic proteins. en MACROPHAGES; DUF59; DOMAIN SWAPPING; PROTEIN-PROTEIN INTERACTIONS; ZINC BINDING Fam96a is a mammalian DUF59 protein, but its structure diverges from those of bacterial DUF59 proteins. Structural clues suggest similarities between Fam96a and amyloidogenic proteins. text/html The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer text