http://journals.iucr.org/f/journalhomepage.html Acta Crystallographica Section F: Structural Biology and Crystallization Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication. en-gb Copyright (c) 2012 International Union of Crystallography International Union of Crystallography International Union of Crystallography http://journals.iucr.org urn:issn:1744-3091 Acta Crystallographica Section F: Structural Biology and Crystallization Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication. text/html Acta Crystallographica Section F Structural Biology and Crystallization Communications text daily 1 2002-01-01T00:00+00:00 med@iucr.org Acta Crystallographica Section F Structural Biology and Crystallization Communications Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 http://journals.iucr.org/logos/rss10f.gif http://journals.iucr.org/f/journalhomepage.html Still image http://journals.iucr.org/f/services/forthcoming.html#fw5365 Crystals of apo-Fur and SeMet-Fur from magnetotactic bacteria M. gryphiswaldense MSR-1 were obtained, and optimized to get high diffraction-quality data. Diffraction data sets were collected and processed at 1.58 and 1.9 Å resolution, respectively. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Liu, Chen and Wu doi: International Union of Crystallography Crystals of apo-Fur and SeMet-Fur from magnetotactic bacteria M. gryphiswaldense MSR-1 were obtained, and optimized to get high diffraction-quality data. Diffraction data sets were collected and processed at 1.58 and 1.9 Å resolution, respectively. en Crystals of apo-Fur and SeMet-Fur from magnetotactic bacteria M. gryphiswaldense MSR-1 were obtained, and optimized to get high diffraction-quality data. Diffraction data sets were collected and processed at 1.58 and 1.9 Å resolution, respectively. text/html Crystallization and preliminary X-ray studies of Ferric Uptake Regulator in Magnetospirillum gryphiswaldense text http://journals.iucr.org/f/services/forthcoming.html#en5496 Crystals of the native and Se-Met labeled STING138–344 proteins from Mus musculus diffracted to resolutions of 2.39 Å and 2.2 Å, respectively Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Yi-Che Su et al. doi: International Union of Crystallography Crystals of the native and Se-Met labeled STING138–344 proteins from Mus musculus diffracted to resolutions of 2.39 Å and 2.2 Å, respectively en STING; C-DI-GMP; INNATE IMMUNE RESPONSE; PATHOGEN; X-RAY CRYSTALLOGRAPHY Crystals of the native and Se-Met labeled STING138–344 proteins from Mus musculus diffracted to resolutions of 2.39 Å and 2.2 Å, respectively text/html Crystallization Studies of the Murine c-di-GMP Sensor Protein STING text http://journals.iucr.org/f/services/forthcoming.html#wd5177 A device has been developed to optimize crystal-growth conditions by experiments in a single drop. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Arne Meyer et al. doi: International Union of Crystallography A device has been developed to optimize crystal-growth conditions by experiments in a single drop. en A device has been developed to optimize crystal-growth conditions by experiments in a single drop. text/html Single-Drop Optimization of Protein Crystallization text http://journals.iucr.org/f/services/forthcoming.html#pg5002 Crystallization Communications Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Fan Zhang et al. doi: International Union of Crystallography Crystallization Communications en YAFN/YAFO COMPLEX; TOXIN-ANTITOXIN SYSTEM; MRNA INTERFERASE Crystallization Communications text/html Crystallization and Preliminary Crystallographic Studies of YafN-YafO Complex from Escherichia coli text http://journals.iucr.org/f/services/forthcoming.html#dp5023 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Shaowei Liu et al. doi: International Union of Crystallography en text/html The expression, crystallization and preliminary crystallographic data analysis of PigF, an O-methyl transferase of prodigiosin synthetic pathway from Serratia text http://journals.iucr.org/f/services/forthcoming.html#dp5027 One protease involved in turnover of Photosynthesis reaction center protein has been crystallized and preliminary diffraction analysis was performed. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Haitian Fan et al. doi: International Union of Crystallography One protease involved in turnover of Photosynthesis reaction center protein has been crystallized and preliminary diffraction analysis was performed. en DEG5; PHOTOSYSTEM II One protease involved in turnover of Photosynthesis reaction center protein has been crystallized and preliminary diffraction analysis was performed. text/html Expression, purification, crystallization and preliminary X-ray diffraction analysis of Deg5 from Arabidopsis thaliana text http://journals.iucr.org/f/services/forthcoming.html#nj5125 Na-FAR-1, a fatty acid and retinol binding protein was expressed in bacteria, purified and crystallized. Crystals grew with two different morphologies under the same conditions. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Mads Gabrielsen et al. doi: International Union of Crystallography Na-FAR-1, a fatty acid and retinol binding protein was expressed in bacteria, purified and crystallized. Crystals grew with two different morphologies under the same conditions. en FATTY-ACID AND RETINOL BINDING PROTEIN; PARASITIC NEMATODE; NECATOR AMERICANUS; NA-FAR-1 Na-FAR-1, a fatty acid and retinol binding protein was expressed in bacteria, purified and crystallized. Crystals grew with two different morphologies under the same conditions. text/html Two crystal forms of a helix-rich fatty acid and retinol-binding protein, Na-FAR-1, from the parasitic nematode Necator americanus text http://journals.iucr.org/f/services/forthcoming.html#pu5371 To characterize the ISP family of proteins present in apicomplexan parasites, ISP1 from T. gondii was expressed, purified, and crystallized. Two crystal forms (cubic and orthorhombic) were analyzed by X-ray diffraction and data were processed to 2.05 and 2.1 Å resolution, respectively. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Michelle L. Tonkin et al. doi: International Union of Crystallography To characterize the ISP family of proteins present in apicomplexan parasites, ISP1 from T. gondii was expressed, purified, and crystallized. Two crystal forms (cubic and orthorhombic) were analyzed by X-ray diffraction and data were processed to 2.05 and 2.1 Å resolution, respectively. en To characterize the ISP family of proteins present in apicomplexan parasites, ISP1 from T. gondii was expressed, purified, and crystallized. Two crystal forms (cubic and orthorhombic) were analyzed by X-ray diffraction and data were processed to 2.05 and 2.1 Å resolution, respectively. text/html Purification, crystallization, and preliminary X-ray diffraction analysis of Inner Membrane Complex (IMC) Sub-compartment Protein 1 (ISP1) from Toxoplasma gondii text http://journals.iucr.org/f/services/forthcoming.html#xb5060 In this work, we report the purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of δ-COP, a medium-sized subunit of COPI complex. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Kai Deng et al. doi: International Union of Crystallography In this work, we report the purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of δ-COP, a medium-sized subunit of COPI complex. en COPI COMPLEX; [DELTA]-COP-CTD; MEMBRANE TRAFFICKING. In this work, we report the purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of δ-COP, a medium-sized subunit of COPI complex. text/html Crystallization and preliminary X-ray analysis of the C-terminal domain of delta-COP, a medium-sized subunit of COPI complex involved in membrane trafficking text http://journals.iucr.org/f/services/forthcoming.html#fw5359 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Tanner and Prag doi: International Union of Crystallography en EPSIN; ENTH DOMAIN; UBIQUITYLATION / CLATHRIN DEPENDENT ENDOCYTOSIS text/html Purification and crystallization of yeast Ent1-ENTH domain text http://journals.iucr.org/f/services/forthcoming.html#bo5105 The expression, purification and crystallization of an N-terminal fragment of SHARPIN are reported. Diffraction-quality crystals were obtained using a 2-D grid screen seeding technique. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Benjamin Stieglitz et al. doi: International Union of Crystallography The expression, purification and crystallization of an N-terminal fragment of SHARPIN are reported. Diffraction-quality crystals were obtained using a 2-D grid screen seeding technique. en CRYSTALLIZATION; SHARPIN; SEEDS. The expression, purification and crystallization of an N-terminal fragment of SHARPIN are reported. Diffraction-quality crystals were obtained using a 2-D grid screen seeding technique. text/html Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization text http://journals.iucr.org/f/services/forthcoming.html#nj5124 Construct engineering and crystallization of E. coli PgaB using in situ proteolysis and mass spectrometry. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Dustin J. Little et al. doi: International Union of Crystallography Construct engineering and crystallization of E. coli PgaB using in situ proteolysis and mass spectrometry. en IN SITU PROTEOLYSIS CRYSTALLIZATION; PROTEIN MODIFICATION AND TRUNCATION; MASS SPECTROMETRY; PGAB; POLY [BETA]-1; 6-N-ACETYL-D-GLUCOSAMINE DEACETYLASE. Construct engineering and crystallization of E. coli PgaB using in situ proteolysis and mass spectrometry. text/html Combining in situ proteolysis and mass spectrometry to crystallize Escherichia coli PgaB text http://journals.iucr.org/f/services/forthcoming.html#hc5146 The Staphylococcus epidermidis carrier protein DltC has been crystallized in order to elucidate the functional role of DltC in the alanylation of lipoteichoic acids in bacteria. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Chi-Hung Huang et al. doi: International Union of Crystallography The Staphylococcus epidermidis carrier protein DltC has been crystallized in order to elucidate the functional role of DltC in the alanylation of lipoteichoic acids in bacteria. en D-ALANYL LIPOTEICHOIC ACIDS; LIPOTEICHOIC ACIDS; STAPHYLOCOCCUS EPIDERMIDIS The Staphylococcus epidermidis carrier protein DltC has been crystallized in order to elucidate the functional role of DltC in the alanylation of lipoteichoic acids in bacteria. text/html Expression, purification, crystallization, and preliminary X-ray analysis of the d-alanyl carrier protein DltC from Staphylococcus epidermidis text http://journals.iucr.org/f/services/forthcoming.html#nj5123 Crystallization of the human NORE1 SARAH domain Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Hye Jin Kim et al. doi: International Union of Crystallography Crystallization of the human NORE1 SARAH domain en NORE1; APOPTOSIS; TUMOR SUPPRESSOR; RAS Crystallization of the human NORE1 SARAH domain text/html Expression, purification, crystallization, and preliminary X-ray analysis of the human NORE1 SARAH domain text http://journals.iucr.org/f/services/forthcoming.html#xb5056 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Han, Liu, Liu and Qiu doi: International Union of Crystallography en text/html Purification, crystallization, and preliminary X-ray diffraction analysis of effector protein PevD1 from Verticillium dahliae text http://journals.iucr.org/f/services/forthcoming.html#uo5039 An ice-binding protein, FfIBP, from Flavobacterium frigoris PS1 was over-expressed, purified and characterized. In addition, the crystallization and preliminary X-ray crystallographic analysis of this ice-binding protein were performed. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Do, Lee, Lee and Kim doi: International Union of Crystallography An ice-binding protein, FfIBP, from Flavobacterium frigoris PS1 was over-expressed, purified and characterized. In addition, the crystallization and preliminary X-ray crystallographic analysis of this ice-binding protein were performed. en ANTIFREEZE PROTEIN; ICE-BINDING PROTEIN; FLAVOBACTERIUM FRIGORIS PS1; PSYCHROPHILIC BACTERIA; X-RAY CRYSTALLOGRAPHY An ice-binding protein, FfIBP, from Flavobacterium frigoris PS1 was over-expressed, purified and characterized. In addition, the crystallization and preliminary X-ray crystallographic analysis of this ice-binding protein were performed. text/html Crystallization and preliminary X-ray crystallographic analysis of an ice-binding protein (FfIBP) from Flavobacterium frigoris PS1 text http://journals.iucr.org/f/services/forthcoming.html#wd5182 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Sebastian Himmel et al. doi: International Union of Crystallography en text/html Structure of the RBD-PRDI fragment of the antiterminator protein GlcT text http://journals.iucr.org/f/services/forthcoming.html#pu5363 The cloning, overexpression, purification, crystallization in a triclinic space group and preliminary X-ray diffraction analysis of the high-molecular-weight ketoacyl reductase FabG4 complexed with NADH are reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Dutta et al. doi:10.1107/S1744309112020301 International Union of Crystallography The cloning, overexpression, purification, crystallization in a triclinic space group and preliminary X-ray diffraction analysis of the high-molecular-weight ketoacyl reductase FabG4 complexed with NADH are reported. en The cloning, overexpression, purification, crystallization in a triclinic space group and preliminary X-ray diffraction analysis of the high-molecular-weight ketoacyl reductase FabG4 complexed with NADH are reported. text/html Crystallization and preliminary X-ray diffraction analysis of the high-molecular-weight ketoacyl reductase FabG4 complexed with NADH text http://journals.iucr.org/f/services/forthcoming.html#bo5106 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Baretta et al. doi:10.1107/S1744309112020222 International Union of Crystallography en PHOSPHOGLYCERATE KINASE; ACINETOBACTER BAUMANNII text/html Expression, purification, crystallization and preliminary crystallographic analysis of the phosphoglycerate kinase from Acinetobacter baumannii text http://journals.iucr.org/f/services/forthcoming.html#pu5373 The putative adhesion domain of the multidomain protein Epf from S. pyogenes has been crystallized in space groups P21 and P212121. The crystals diffracted to 2.0 and 1.6 Å resolution, respectively, at the Australian Synchrotron. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Linke et al. doi:10.1107/S1744309112020313 International Union of Crystallography The putative adhesion domain of the multidomain protein Epf from S. pyogenes has been crystallized in space groups P21 and P212121. The crystals diffracted to 2.0 and 1.6 Å resolution, respectively, at the Australian Synchrotron. en The putative adhesion domain of the multidomain protein Epf from S. pyogenes has been crystallized in space groups P21 and P212121. The crystals diffracted to 2.0 and 1.6 Å resolution, respectively, at the Australian Synchrotron. text/html Purification, crystallization and preliminary crystallographic analysis of the adhesion domain of Epf from Streptococcus pyogenes text http://journals.iucr.org/f/services/forthcoming.html#ub5031 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Lopez-Zavala et al. doi:10.1107/S1744309112020180 International Union of Crystallography en text/html Crystallization and X-ray diffraction studies of white Pacific shrimp Litopenaeus vannamei arginine kinase text http://journals.iucr.org/f/services/forthcoming.html#fw5364 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Henrick & Hirshberg doi:10.1107/S1744309112020167 International Union of Crystallography en TRAP; STAPHYLOCOCCUS AUREUS; SIGNAL TRANSDUCTION text/html Structure of the signal transduction protein TRAP (target of RNAIII-activating protein) text http://journals.iucr.org/f/services/forthcoming.html#ft5024 The extracellular region of mouse Enpp1 was expressed, purified and crystallized. An X-ray diffraction data set was collected to 3.0 Å resolution by employing a helical data-collection strategy involving a micro-focus synchrotron beam. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Kato et al. doi:10.1107/S1744309112019306 International Union of Crystallography The extracellular region of mouse Enpp1 was expressed, purified and crystallized. An X-ray diffraction data set was collected to 3.0 Å resolution by employing a helical data-collection strategy involving a micro-focus synchrotron beam. en ENPP1 The extracellular region of mouse Enpp1 was expressed, purified and crystallized. An X-ray diffraction data set was collected to 3.0 Å resolution by employing a helical data-collection strategy involving a micro-focus synchrotron beam. text/html Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp1 text http://journals.iucr.org/f/services/forthcoming.html#pu5368 This paper reports the cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of acyl-protein thioesterase 1 from S. cerevisiae. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Yuan et al. doi:10.1107/S1744309112019276 International Union of Crystallography This paper reports the cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of acyl-protein thioesterase 1 from S. cerevisiae. en PALMITOYLATION; ACYL-PROTEIN THIOESTERASE 1; SACCHAROMYCES CEREVISIAE This paper reports the cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of acyl-protein thioesterase 1 from S. cerevisiae. text/html Cloning, purification, crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae text http://journals.iucr.org/f/services/forthcoming.html#tb5050 A crystallographic and biochemical study of L. major cysteine synthase, which is a pyridoxyl phosphate-dependent enzyme, is reported. The structure was determined to 1.8 Å resolution and revealed that the cofactor has been lost and that a fragment of γ-poly-d-glutamic acid, a crystallization ingredient, was bound in the active site. The enzyme was inhibited by peptides. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Fyfe et al. doi:10.1107/S1744309112019124 International Union of Crystallography A crystallographic and biochemical study of L. major cysteine synthase, which is a pyridoxyl phosphate-dependent enzyme, is reported. The structure was determined to 1.8 Å resolution and revealed that the cofactor has been lost and that a fragment of γ-poly-d-glutamic acid, a crystallization ingredient, was bound in the active site. The enzyme was inhibited by peptides. en ARABIDOPSIS THALIANA; CYSTEINE SYNTHASE; LEISHMANIA MAJOR A crystallographic and biochemical study of L. major cysteine synthase, which is a pyridoxyl phosphate-dependent enzyme, is reported. The structure was determined to 1.8 Å resolution and revealed that the cofactor has been lost and that a fragment of γ-poly-d-glutamic acid, a crystallization ingredient, was bound in the active site. The enzyme was inhibited by peptides. text/html Structure of Leishmania major cysteine synthase text http://journals.iucr.org/f/services/forthcoming.html#fw5360 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Nakano et al. doi:10.1107/S1744309112018969 International Union of Crystallography en PZ PEPTIDASE B; GEOBACILLUS COLLAGENOVARANS MO-1; MICROGRAVITY text/html Crystallization and preliminary X-ray crystallographic analysis of Pz peptidase B from Geobacillus collagenovarans MO-1 text http://journals.iucr.org/f/services/forthcoming.html#dp5024 A hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase involved in chlorogenic acid biosynthesis in C. canephora was crystallized using the vapour-diffusion method. A diffraction data set was collected to 3.0 Å resolution on the microfocus beamline (ID23-2) at ESRF and a structure solution was obtained using molecular replacement. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Lallemand et al. doi:10.1107/S1744309112019082 International Union of Crystallography A hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase involved in chlorogenic acid biosynthesis in C. canephora was crystallized using the vapour-diffusion method. A diffraction data set was collected to 3.0 Å resolution on the microfocus beamline (ID23-2) at ESRF and a structure solution was obtained using molecular replacement. en COFFEA CANEPHORA; PHENYLPROPANOID-BIOSYNTHESIS PATHWAY; CHLOROGENIC ACIDS; PLANT ACYL-COA-DEPENDENT ACYLTRANSFERASE SUPERFAMILY; HYDROXYCINNAMOYL-COA SHIKIMATE/QUINATE HYDROXYCINNAMOYLTRANSFERASE; MOLECULAR REPLACEMENT A hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase involved in chlorogenic acid biosynthesis in C. canephora was crystallized using the vapour-diffusion method. A diffraction data set was collected to 3.0 Å resolution on the microfocus beamline (ID23-2) at ESRF and a structure solution was obtained using molecular replacement. text/html Purification, crystallization and preliminary X-ray diffraction analysis of a hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase (HCT) from Coffea canephora involved in chlorogenic acid biosynthesis text http://journals.iucr.org/f/services/forthcoming.html#ft5022 Nonstructural protein 2 from avian infectious bronchitis virus has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.8 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Yu et al. doi:10.1107/S1744309112018623 International Union of Crystallography Nonstructural protein 2 from avian infectious bronchitis virus has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.8 Å resolution. en AVIAN INFECTIOUS BRONCHITIS VIRUS; NONSTRUCTURAL PROTEIN 2 Nonstructural protein 2 from avian infectious bronchitis virus has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.8 Å resolution. text/html Purification, crystallization and preliminary X-ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus text http://journals.iucr.org/f/services/forthcoming.html#ub5032 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Buysschaert et al. doi:10.1107/S1744309112018672 International Union of Crystallography en SHORT-CHAIN DEHYDROGENASES/REDUCTASES; VIBRIO VULNIFICUS text/html Crystallization of an atypical short-chain dehydrogenase from Vibrio vulnificus lacking the conserved catalytic tetrad text http://journals.iucr.org/f/services/forthcoming.html#uo5036 T. maritima CheA P3-P4-P5 domains were crystallized in complex with CheW. Low-resolution diffraction data were collected to ∼8 Å using synchrotron X-ray radiation. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Park et al. doi:10.1107/S174430911201826X International Union of Crystallography T. maritima CheA P3-P4-P5 domains were crystallized in complex with CheW. Low-resolution diffraction data were collected to ∼8 Å using synchrotron X-ray radiation. en CHEA; HISTIDINE KINASES; CHEW; COUPLING PROTEINS; BACTERIAL CHEMOTAXIS; SIGNAL TRANSDUCTION; THERMOTOGA MARITIMA T. maritima CheA P3-P4-P5 domains were crystallized in complex with CheW. Low-resolution diffraction data were collected to ∼8 Å using synchrotron X-ray radiation. text/html Crystallization and preliminary X-ray crystallographic analysis of Thermotoga maritima CheA P3-P4-P5 domains in complex with CheW text http://journals.iucr.org/f/services/forthcoming.html#fw5363 Cyclophin A like protein from Piriformospora indica involved in salt-stress tolerance was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 2 Å resolution and belonged to space group C2221. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Bhatt et al. doi:10.1107/S1744309112018131 International Union of Crystallography Cyclophin A like protein from Piriformospora indica involved in salt-stress tolerance was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 2 Å resolution and belonged to space group C2221. en CYCLOPHILIN A; PIRIFORMOSPORA INDICA; SALINITY STRESS Cyclophin A like protein from Piriformospora indica involved in salt-stress tolerance was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 2 Å resolution and belonged to space group C2221. text/html Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of a cyclophilin A-like protein from Piriformospora indica text http://journals.iucr.org/f/services/forthcoming.html#tt5029 The crystal structure of a short-chain dehydrogenase/reductase from B. anthracis strain `Ames Ancestor' is reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Hou et al. doi:10.1107/S1744309112017939 International Union of Crystallography The crystal structure of a short-chain dehydrogenase/reductase from B. anthracis strain `Ames Ancestor' is reported. en SHORT-CHAIN DEHYDROGENASES/REDUCTASES; NADP; BACILLUS ANTHRACIS The crystal structure of a short-chain dehydrogenase/reductase from B. anthracis strain `Ames Ancestor' is reported. text/html Structure of a short-chain dehydrogenase/reductase from Bacillus anthracis text http://journals.iucr.org/f/services/forthcoming.html#xb5050 Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Chen et al. doi:10.1107/S1744309112017812 International Union of Crystallography en FERULOYL ESTERASE text/html Crystallization and preliminary X-ray analysis of a novel halotolerant feruloyl esterase identified from a soil metagenomic library text http://journals.iucr.org/f/services/forthcoming.html#hc5145 The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction data are described for UDP-galactopyranose mutase, an enzyme involved in cell-wall synthesis in A. fumigatus. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Penman et al. doi:10.1107/S1744309112017915 International Union of Crystallography The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction data are described for UDP-galactopyranose mutase, an enzyme involved in cell-wall synthesis in A. fumigatus. en UDP-GALACTOPYRANOSE MUTASE; ASPERGILLUS FUMIGATUS The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction data are described for UDP-galactopyranose mutase, an enzyme involved in cell-wall synthesis in A. fumigatus. text/html Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus text http://journals.iucr.org/f/services/forthcoming.html#kw5039 The structure of the L166K variant of G protein-coupled receptor kinase 1 has been determined at 2.5 Å resolution in order to determine how a dimer interface observed in prior crystal structures influences the conformation of the enzyme and how the C-terminal amino acids are configured while in a monomeric state. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Tesmer et al. doi:10.1107/S1744309112017435 International Union of Crystallography The structure of the L166K variant of G protein-coupled receptor kinase 1 has been determined at 2.5 Å resolution in order to determine how a dimer interface observed in prior crystal structures influences the conformation of the enzyme and how the C-terminal amino acids are configured while in a monomeric state. en RHODOPSIN KINASE; GRK1; RGS HOMOLOGY DOMAIN; DIMERIZATION The structure of the L166K variant of G protein-coupled receptor kinase 1 has been determined at 2.5 Å resolution in order to determine how a dimer interface observed in prior crystal structures influences the conformation of the enzyme and how the C-terminal amino acids are configured while in a monomeric state. text/html Structure of a monomeric variant of rhodopsin kinase at 2.5 Å resolution text http://journals.iucr.org/f/services/forthcoming.html#nj5120 The JmjC domain-containing histone demethylase NO66 from H. sapiens was overproduced in E. coli, purified and crystallized. Diffraction data were collected to 2.29 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Zhou et al. doi:10.1107/S174430911201740X International Union of Crystallography The JmjC domain-containing histone demethylase NO66 from H. sapiens was overproduced in E. coli, purified and crystallized. Diffraction data were collected to 2.29 Å resolution. en HISTONE DEMETHYLASES; NO66; JMJC DOMAIN The JmjC domain-containing histone demethylase NO66 from H. sapiens was overproduced in E. coli, purified and crystallized. Diffraction data were collected to 2.29 Å resolution. text/html Purification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 from Homo sapiens text http://journals.iucr.org/f/services/forthcoming.html#nj5118 Recombinant Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-­adenosyl-l-methionine-dependent C-methyltransferase, has been successfully cloned, expressed and purified. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Lyskowski et al. doi:10.1107/S1744309112017137 International Union of Crystallography Recombinant Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-­adenosyl-l-methionine-dependent C-methyltransferase, has been successfully cloned, expressed and purified. en COUO; METHYLTRANSFERASES; S-ADENOSYL-L-METHIONINE; STREPTOMYCES RISHIRIENSIS Recombinant Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-­adenosyl-l-methionine-dependent C-methyltransferase, has been successfully cloned, expressed and purified. text/html Crystallization of the novel S-adenosyl-l-methionine-dependent C-methyltransferase CouO from Streptomyces rishiriensis and preliminary diffraction data analysis text http://journals.iucr.org/f/services/forthcoming.html#gj5103 A mutated version of InsP5 2-K allows the production of crystals of the apo form and structure determination using X-ray crystallography. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Baños-Sanz et al. doi:10.1107/S1744309112017307 International Union of Crystallography A mutated version of InsP5 2-K allows the production of crystals of the apo form and structure determination using X-ray crystallography. en INOSITOL KINASES; INOSITOL PHOSPHATE; PHYTIC ACID; IP6; IP5 2-K A mutated version of InsP5 2-K allows the production of crystals of the apo form and structure determination using X-ray crystallography. text/html Expression, purification, crystallization and preliminary X-ray diffraction analysis of the apo form of InsP5 2-K from Arabidopsis thaliana text http://journals.iucr.org/f/services/forthcoming.html#rl5018 MvfRC87, a 242-residue C-­terminal segment of the LysR-type transcriptional regulator MvfR, was produced in Escherichia coli, purified and crystallized. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Kefala et al. doi:10.1107/S1744309112016661 International Union of Crystallography MvfRC87, a 242-residue C-­terminal segment of the LysR-type transcriptional regulator MvfR, was produced in Escherichia coli, purified and crystallized. en MVFR; LYSR-TYPE TRANSCRIPTIONAL REGULATORS; PSEUDOMONAS AERUGINOSA MvfRC87, a 242-residue C-­terminal segment of the LysR-type transcriptional regulator MvfR, was produced in Escherichia coli, purified and crystallized. text/html Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa text http://journals.iucr.org/f/services/forthcoming.html#dp5021 The reductase component of p-hydroxyphenylacetate 3-hydroxylase from A. baumannii was overexpressed, purified and crystallized. X-ray diffraction data were collected and processed to 2.3 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Oonanant et al. doi:10.1107/S1744309112016909 International Union of Crystallography The reductase component of p-hydroxyphenylacetate 3-hydroxylase from A. baumannii was overexpressed, purified and crystallized. X-ray diffraction data were collected and processed to 2.3 Å resolution. en ACINETOBACTER BAUMANNII; FLAVIN REDUCTASES; P-HYDROXYPHENYLACETATE; P-HYDROXYPHENYLACETATE 3-HYDROXYLASE; TWO-COMPONENT FLAVOPROTEINS The reductase component of p-hydroxyphenylacetate 3-hydroxylase from A. baumannii was overexpressed, purified and crystallized. X-ray diffraction data were collected and processed to 2.3 Å resolution. text/html Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii text http://journals.iucr.org/f/services/forthcoming.html#pg5003 The complex of CCM3 and the C-terminal domain of MST4 has been successfully constructed, purified and crystallized. The crystal diffracted to a resolution of 2.4 Å. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Xu et al. doi:10.1107/S1744309112016843 International Union of Crystallography The complex of CCM3 and the C-terminal domain of MST4 has been successfully constructed, purified and crystallized. The crystal diffracted to a resolution of 2.4 Å. en CEREBRAL CAVERNOUS MALFORMATIONS; GCKIII KINASES; CCM3-MST4 C-TERMINAL DOMAIN COMPLEX The complex of CCM3 and the C-terminal domain of MST4 has been successfully constructed, purified and crystallized. The crystal diffracted to a resolution of 2.4 Å. text/html Crystallization and preliminary crystallographic studies of CCM3 in complex with the C-terminal domain of MST4 text http://journals.iucr.org/f/services/forthcoming.html#dp5022 Rv0864, an enzyme of the Moco biosynthesis pathway from M. tuberculosis, has been overexpressed, purified and crystallized. Diffraction data to 2.5 Å were collected and the structure solved by molecular replacement. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Srivastava et al. doi:10.1107/S174430911201665X International Union of Crystallography Rv0864, an enzyme of the Moco biosynthesis pathway from M. tuberculosis, has been overexpressed, purified and crystallized. Diffraction data to 2.5 Å were collected and the structure solved by molecular replacement. en MOAC2; MYCOBACTERIUM TUBERCULOSIS H37RV; MOLYBDENUM COFACTOR BIOSYNTHESIS Rv0864, an enzyme of the Moco biosynthesis pathway from M. tuberculosis, has been overexpressed, purified and crystallized. Diffraction data to 2.5 Å were collected and the structure solved by molecular replacement. text/html Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv text http://journals.iucr.org/f/services/forthcoming.html#no5004 Here, the expression, purification, crystallization and preliminary crystallographic analysis of human α1m are reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Zhang et al. doi:10.1107/S1744309112016569 International Union of Crystallography Here, the expression, purification, crystallization and preliminary crystallographic analysis of human α1m are reported. en [ALPHA]1-MICROGLOBULIN; LIPOCALINS Here, the expression, purification, crystallization and preliminary crystallographic analysis of human α1m are reported. text/html Cloning, purification, crystallization and preliminary X-ray studies of human α1-microglobulin text http://journals.iucr.org/f/services/forthcoming.html#ft5021 The GhKCH2 motor domain was crystallized and the pH of the crystallization buffer was shown to have a significant effect on the crystal morphology and diffraction quality. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Qin et al. doi:10.1107/S1744309112016351 International Union of Crystallography The GhKCH2 motor domain was crystallized and the pH of the crystallization buffer was shown to have a significant effect on the crystal morphology and diffraction quality. en KINESINS; PH; CRYSTAL MORPHOLOGY; DIFFRACTION QUALITY The GhKCH2 motor domain was crystallized and the pH of the crystallization buffer was shown to have a significant effect on the crystal morphology and diffraction quality. text/html Crystallization and preliminary X-ray diffraction studies of the GhKCH2 motor domain: alteration of pH significantly improved the quality of the crystals text http://journals.iucr.org/f/services/forthcoming.html#gx5204 The structure of 3-methyladenine DNA glycosylase I in complex with 3-methyladenine is reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Zhu et al. doi:10.1107/S1744309112016363 International Union of Crystallography The structure of 3-methyladenine DNA glycosylase I in complex with 3-methyladenine is reported. en 3-METHYLADENINE DNA GLYCOSYLASE I; FLUORESCENCE MEASUREMENTS; ITC; DNA REPAIR; RECOGNITION The structure of 3-methyladenine DNA glycosylase I in complex with 3-methyladenine is reported. text/html A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus text http://journals.iucr.org/f/services/forthcoming.html#rl5020 The purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of CCM2, which is part of a signalling complex, are reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Wang et al. doi:10.1107/S1744309112016181 International Union of Crystallography The purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of CCM2, which is part of a signalling complex, are reported. en CEREBRAL CAVERNOUS MALFORMATIONS; ADAPTOR PROTEINS; KARET DOMAINS; SIGNALLING PATHWAYS The purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of CCM2, which is part of a signalling complex, are reported. text/html Crystallization and preliminary X-ray analysis of the C-terminal domain of CCM2, part of a novel adaptor protein involved in cerebral cavernous malformations text http://journals.iucr.org/f/services/forthcoming.html#uo5038 Bacterial selenocysteine tRNA was crystallized as the heterologous complex with archaeal seryl-tRNA synthetase. X-ray diffraction was improved by introducing point mutations and heavy-atom labeling, and a 3.2 Å diffraction data set for phase determination was obtained from a platinum-labeled crystal. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Itoh et al. doi:10.1107/S1744309112016004 International Union of Crystallography Bacterial selenocysteine tRNA was crystallized as the heterologous complex with archaeal seryl-tRNA synthetase. X-ray diffraction was improved by introducing point mutations and heavy-atom labeling, and a 3.2 Å diffraction data set for phase determination was obtained from a platinum-labeled crystal. en SERYL-TRNA SYNTHETASE; TRNASEC Bacterial selenocysteine tRNA was crystallized as the heterologous complex with archaeal seryl-tRNA synthetase. X-ray diffraction was improved by introducing point mutations and heavy-atom labeling, and a 3.2 Å diffraction data set for phase determination was obtained from a platinum-labeled crystal. text/html Crystallization and preliminary X-ray crystallographic analysis of bacterial tRNASec in complex with seryl-tRNA synthetase text http://journals.iucr.org/f/services/forthcoming.html#hc5142 P. falciparum GTP:AMP phosphotransferase was expressed in E. coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 2.90 Å. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Law et al. doi:10.1107/S1744309112015862 International Union of Crystallography P. falciparum GTP:AMP phosphotransferase was expressed in E. coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 2.90 Å. en GTP:AMP PHOSPHOTRANSFERASE; PLASMODIUM FALCIPARUM; ADENYLATE KINASES P. falciparum GTP:AMP phosphotransferase was expressed in E. coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 2.90 Å. text/html Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase text http://journals.iucr.org/f/services/forthcoming.html#fw5361 Human histidine decarboxylase was crystallized by the sitting-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Komori et al. doi:10.1107/S1744309112015692 International Union of Crystallography Human histidine decarboxylase was crystallized by the sitting-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution. en HUMAN HISTIDINE DECARBOXYLASE; HISTAMINE; PYRIDOXAL 5'-PHOSPHATE-DEPENDENT ENZYMES Human histidine decarboxylase was crystallized by the sitting-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution. text/html Purification, crystallization and preliminary X-ray analysis of human histidine decarboxylase text http://journals.iucr.org/f/services/forthcoming.html#no5002 The catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme–inhibitor complex was refined to 2.1 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Hall et al. doi:10.1107/S1744309112015618 International Union of Crystallography The catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme–inhibitor complex was refined to 2.1 Å resolution. en ADAM-8; METALLOPROTEASES; INHIBITORS; BATIMASTAT; INFLAMMATION The catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme–inhibitor complex was refined to 2.1 Å resolution. text/html Structure of human ADAM-8 catalytic domain complexed with batimastat text http://journals.iucr.org/f/services/forthcoming.html#pu5369 Human peptidylarginine deiminase type III was crystallized using polyethylene glycol monomethylether or polyethylene glycol as a precipitant. The crystals belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes), and contained two molecules in an asymmetric unit. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Unno et al. doi:10.1107/S1744309112015333 International Union of Crystallography Human peptidylarginine deiminase type III was crystallized using polyethylene glycol monomethylether or polyethylene glycol as a precipitant. The crystals belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes), and contained two molecules in an asymmetric unit. en PEPTIDYLARGININE DEIMINASE III; CITRULLINATION; PROTEIN-MODIFYING ENZYMES; DIMERS Human peptidylarginine deiminase type III was crystallized using polyethylene glycol monomethylether or polyethylene glycol as a precipitant. The crystals belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes), and contained two molecules in an asymmetric unit. text/html Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type III text http://journals.iucr.org/f/services/forthcoming.html#bo5104 Crystals of the complex of E. coli O157 ParE2 and PaaA2 belong to space group P3121 or P3221 and diffract to 3.8 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Sterckx et al. doi:10.1107/S1744309112015230 International Union of Crystallography Crystals of the complex of E. coli O157 ParE2 and PaaA2 belong to space group P3121 or P3221 and diffract to 3.8 Å resolution. en TOXIN-ANTITOXIN MODULES; GYRASE POISONS; INTRINSIC DISORDER Crystals of the complex of E. coli O157 ParE2 and PaaA2 belong to space group P3121 or P3221 and diffract to 3.8 Å resolution. text/html The ParE2–PaaA2 toxin–antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal text http://journals.iucr.org/f/services/forthcoming.html#nj5121 The expression, purification and crystallization of the soluble forms of LukE and LukD, which together constitute the LukE–LukD staphylococcal leukotoxin, are described. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Galy et al. doi:10.1107/S1744309112014662 International Union of Crystallography The expression, purification and crystallization of the soluble forms of LukE and LukD, which together constitute the LukE–LukD staphylococcal leukotoxin, are described. en LEUKOTOXINS; STAPHYLOCOCCUS AUREUS The expression, purification and crystallization of the soluble forms of LukE and LukD, which together constitute the LukE–LukD staphylococcal leukotoxin, are described. text/html Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE–LukD leukotoxin text http://journals.iucr.org/f/services/forthcoming.html#nj5119 The collection of X-ray diffraction data from malate dehydrogenase from P. falciparum to a resolution of 2.2 Å is reported. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Wrenger et al. doi:10.1107/S1744309112014571 International Union of Crystallography The collection of X-ray diffraction data from malate dehydrogenase from P. falciparum to a resolution of 2.2 Å is reported. en PLASMODIUM FALCIPARUM; CARBON METABOLISM; ENERGY METABOLISM; RESPIRATORY CHAIN; MALATE DEHYDROGENASE The collection of X-ray diffraction data from malate dehydrogenase from P. falciparum to a resolution of 2.2 Å is reported. text/html Crystallization and preliminary X-ray diffraction of malate dehydrogenase from Plasmodium falciparum text http://journals.iucr.org/f/services/forthcoming.html#pu5356 The haloalkane dehalogenase DatA from A. tumefaciens C58 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.70 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Mase et al. doi:10.1107/S1744309112013942 International Union of Crystallography The haloalkane dehalogenase DatA from A. tumefaciens C58 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.70 Å resolution. en HALOALKANE DEHALOGENASES; BIOREMEDIATION The haloalkane dehalogenase DatA from A. tumefaciens C58 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.70 Å resolution. text/html Crystallization and preliminary X-ray analysis of the haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 text http://journals.iucr.org/f/services/forthcoming.html#pu5367 The ATPase domain of human TAP in nucleotide free, ADP, vanadate and azide complexed forms were purified and crystallized. The X-ray diffraction data sets were collected for all crystals in the resolution range of 2.8–3.0 Å. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Meena et al. doi:10.1107/S1744309112013954 International Union of Crystallography The ATPase domain of human TAP in nucleotide free, ADP, vanadate and azide complexed forms were purified and crystallized. The X-ray diffraction data sets were collected for all crystals in the resolution range of 2.8–3.0 Å. en ABC TRANSPORTERS; TAP; ATPASE DOMAIN; CATALYTIC CYCLE The ATPase domain of human TAP in nucleotide free, ADP, vanadate and azide complexed forms were purified and crystallized. The X-ray diffraction data sets were collected for all crystals in the resolution range of 2.8–3.0 Å. text/html Purification, crystallization and preliminary X-ray crystallographic analysis of the ATPase domain of human TAP in nucleotide-free and ADP-, vanadate- and azide-complexed forms text http://journals.iucr.org/f/services/forthcoming.html#hv5215 The structure of the Rem2 G domain bound to GDP is reported in a monoclinic crystal form at 2.66 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Reymond et al. doi:10.1107/S1744309112013541 International Union of Crystallography The structure of the Rem2 G domain bound to GDP is reported in a monoclinic crystal form at 2.66 Å resolution. en SMALL GTP-BINDING PROTEINS; GTPASES; RGK PROTEINS; REM2; G DOMAINS; SWITCH REGIONS; DXWEX MOTIF The structure of the Rem2 G domain bound to GDP is reported in a monoclinic crystal form at 2.66 Å resolution. text/html Structure of the GDP-bound G domain of the RGK protein Rem2 text http://journals.iucr.org/f/services/forthcoming.html#fw5357 d-Aspartate oxidase from porcine kidney was crystallized by the sitting-drop vapour-diffusion method. The crystal diffracted to 1.80 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Senda et al. doi:10.1107/S1744309112013243 International Union of Crystallography d-Aspartate oxidase from porcine kidney was crystallized by the sitting-drop vapour-diffusion method. The crystal diffracted to 1.80 Å resolution. en D-ASPARTATE OXIDASE; FAD; FLAVOPROTEINS; ANAEROBIC CRYSTALLIZATION d-Aspartate oxidase from porcine kidney was crystallized by the sitting-drop vapour-diffusion method. The crystal diffracted to 1.80 Å resolution. text/html Crystallization and preliminary crystallographic analysis of d-aspartate oxidase from porcine kidney text http://journals.iucr.org/f/services/forthcoming.html#ft5023 The amino-terminal domain of the Hsp70 co-chaperone Bag2 from M. musculus has been crystallized in native and selenomethionyl forms diffracting to 2.27 and 3.1 Å resolution, respectively. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Page et al. doi:10.1107/S1744309112013267 International Union of Crystallography The amino-terminal domain of the Hsp70 co-chaperone Bag2 from M. musculus has been crystallized in native and selenomethionyl forms diffracting to 2.27 and 3.1 Å resolution, respectively. en BAG2; SELENOMETHIONINE; SAD PHASING The amino-terminal domain of the Hsp70 co-chaperone Bag2 from M. musculus has been crystallized in native and selenomethionyl forms diffracting to 2.27 and 3.1 Å resolution, respectively. text/html Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus text http://journals.iucr.org/f/services/forthcoming.html#bo5103 MatP is a small DNA-binding protein of about 18 kDa. In order to understand the DNA-compaction mechanism of MatP at an atomic level, the structures of apo MatP and of the nucleoprotein complex MatP–matS have been studied. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Durand et al. doi:10.1107/S1744309112011062 International Union of Crystallography MatP is a small DNA-binding protein of about 18 kDa. In order to understand the DNA-compaction mechanism of MatP at an atomic level, the structures of apo MatP and of the nucleoprotein complex MatP–matS have been studied. en MATP; MATS; DNA-BINDING PROTEINS; ESCHERICHIA COLI MatP is a small DNA-binding protein of about 18 kDa. In order to understand the DNA-compaction mechanism of MatP at an atomic level, the structures of apo MatP and of the nucleoprotein complex MatP–matS have been studied. text/html Expression, purification and preliminary structural analysis of Escherichia coli MatP in complex with the matS DNA site text http://journals.iucr.org/f/services/forthcoming.html#tb5047 The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator, was solved at 2.5 Å resolution. Copyright (c) 2012 International Union of Crystallography urn:issn:1744-3091 Sainsbury et al. doi:10.1107/S1744309112010603 International Union of Crystallography The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator, was solved at 2.5 Å resolution. en METR; NEISSERIA MENINGITIDIS; LYSR-TYPE REGULATOR The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator, was solved at 2.5 Å resolution. text/html Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis text