http://journals.iucr.org/f/issues/2008/09/00/isscontsbdy.html Acta Crystallographica Section F Structural Biology and Crystallization Communications aims to provide a home for communications on the crystallization and structure determination of biological macromolecules. It will commence publication in January 2005 and will include three categories of publication: Structural genomics communications, Protein structure communications, Crystallization communications. Articles will be available online when ready, making publication as fast as possible, and will include unlimited free colour illustrations, movies and other enhancements. The editorial process will be completely electronic with respect to deposition, submission, refereeing and publication. en Copyright (c) 2008 International Union of Crystallography 2008-09-01 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 aims to provide a home for communications on the crystallization and structure determination of biological macromolecules. It will commence publication in January 2005 and will include three categories of publication: Structural genomics communications, Protein structure communications, Crystallization communications. Articles will be available online when ready, making publication as fast as possible, and will include unlimited free colour illustrations, movies and other enhancements. The editorial process will be completely electronic with respect to deposition, submission, refereeing and publication. text/html Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Volume 64, Part 9, 2008 text monthly 1 2002-01-01T00:00+00:00 9 64 2008-09-01 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications 772 urn:issn:1744-3091 med@iucr.org September 2008 2008-09-01 http://journals.iucr.org/logos/rss10f.gif http://journals.iucr.org/f/issues/2008/09/00/isscontsbdy.html Still image http://scripts.iucr.org/cgi-bin/paper?hv5112 Streptococcus pneumoniae genomes encode three sialidases, NanA, NanB and NanC, which are key virulence factors that remove sialic acids from various glycoconjugates. The enzymes have potential as drug targets and also as vaccine candidates. The 115 kDa NanA is the largest of the three sialidases and is anchored to the bacterial membrane. Although recombinantly expressed full-length NanA was soluble, it failed to crystallize; therefore, a 56.5 kDa domain that retained full enzyme activity was subcloned. The purified enzyme was crystallized in 0.1 M MES pH 6.5, 30%(w/v) PEG 4000 using the sitting-drop vapour-diffusion method. Data were collected at 100 K to 2.5 Å resolution from a crystal grown in the presence of the inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. The crystal belongs to space group P212121, with unit-cell parameters a = 49.2, b = 95.6, c = 226.6 Å. The structure was solved by molecular replacement and refined to final R and Rfree factors of 0.246 and 0.298, respectively. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Xu, G. Li, X. Andrew, P.W. Taylor, G.L. 2008-08-20 doi:10.1107/S1744309108024044 International Union of Crystallography The structure of a catalytically active subdomain of the NanA sialidase from S. pneumoniae is reported to a resolution of 2.5 Å. The complex with the inhibitor Neu5Ac2en identifies the key catalytic residues and provides a platform for structure-based development of specific inhibitors. en NanA sialidases Streptococcus pneumoniae Streptococcus pneumoniae genomes encode three sialidases, NanA, NanB and NanC, which are key virulence factors that remove sialic acids from various glycoconjugates. The enzymes have potential as drug targets and also as vaccine candidates. The 115 kDa NanA is the largest of the three sialidases and is anchored to the bacterial membrane. Although recombinantly expressed full-length NanA was soluble, it failed to crystallize; therefore, a 56.5 kDa domain that retained full enzyme activity was subcloned. The purified enzyme was crystallized in 0.1 M MES pH 6.5, 30%(w/v) PEG 4000 using the sitting-drop vapour-diffusion method. Data were collected at 100 K to 2.5 Å resolution from a crystal grown in the presence of the inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. The crystal belongs to space group P212121, with unit-cell parameters a = 49.2, b = 95.6, c = 226.6 Å. The structure was solved by molecular replacement and refined to final R and Rfree factors of 0.246 and 0.298, respectively. text/html Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications protein structure communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5308 Crystals of the catalytic subunit of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes that are similar to each other and to a previously determined monoclinic C2 form. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4° between crystal forms. Moreover, there is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4° between crystal forms. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Vitali, J. Colaneri, M.J. 2008-08-20 doi:10.1107/S1744309108025359 International Union of Crystallography The structure of the catalytic subunit of M. jannaschii aspartate transcarbamoylase has been determined in space group P212121 using synchrotron data to a resolution of 3.0 Å and was refined to a final Rwork and Rfree of 0.215 and 0.269, respectively. en aspartate transcarbamoylase catalytic subunit Methanococcus jannaschii Crystals of the catalytic subunit of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes that are similar to each other and to a previously determined monoclinic C2 form. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4° between crystal forms. Moreover, there is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4° between crystal forms. text/html Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications protein structure communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5160 MASP-1, a multidomain serine protease, is a component of the lectin pathway of complement. Its precise function is unknown, although it seems to enhance the complement-activating capacity of MASP-2, a related enzyme. MASP-1 has also been implicated as playing a role in blood coagulation. It is mostly found associated with mannose-binding lectin (MBL) and ficolins. Early attempts to crystallize MASP-1 failed because of the inhomogeneity of the purified material. MASP-1 was shown by acidic nondenaturing PAGE to be composed of differently charged species, which are most likely to be the products of deamidation occurring during the refolding procedure. Sequential cation-exchange and anion-exchange chromatography resulted in a homogeneous material, which was successfully crystallized. The best crystal diffracted to 2.55 Å resolution and belonged to space group P212121, with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 Å. The crystal structure of MASP-1 may help in understanding the function of this mysterious serine protease. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Dobó, J. Harmat, V. Sebestyén, E. Beinrohr, L. Závodszky, P. Gál, P. 2008-08-09 doi:10.1107/S174430910802294X International Union of Crystallography Acidic nondenaturing PAGE revealed inhomogeneity of the MASP-1 catalytic region caused by deamidation as the reason behind previous unsuccessful crystallization attempts. Monitoring the separation of the various species by acidic nondenaturing PAGE during purification helped to obtain pure protein, which was subsequently crystallized. en innate immunity complement-control protein domain modular serine proteases mannan-binding lectins collectins acidic PAGE MASP-1, a multidomain serine protease, is a component of the lectin pathway of complement. Its precise function is unknown, although it seems to enhance the complement-activating capacity of MASP-2, a related enzyme. MASP-1 has also been implicated as playing a role in blood coagulation. It is mostly found associated with mannose-binding lectin (MBL) and ficolins. Early attempts to crystallize MASP-1 failed because of the inhomogeneity of the purified material. MASP-1 was shown by acidic nondenaturing PAGE to be composed of differently charged species, which are most likely to be the products of deamidation occurring during the refolding procedure. Sequential cation-exchange and anion-exchange chromatography resulted in a homogeneous material, which was successfully crystallized. The best crystal diffracted to 2.55 Å resolution and belonged to space group P212121, with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 Å. The crystal structure of MASP-1 may help in understanding the function of this mysterious serine protease. text/html Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?nj5018 Histamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe–4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 Å resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 Å. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Reed, T.M. Hirakawa, H. Mure, M. Scott, E.E. Limburg, J. 2008-08-09 doi:10.1107/S1744309108023336 International Union of Crystallography Histamine dehydrogenase from Nocardioides simplex has been expressed, purified and crystallized with full incorporation of 6-S-cysteinyl-FMN. Diffraction data has been collected to 2.7–Å resolution with the crystals belonging to the orthorhombic space group P212121. en histamine dehydrogenase Nocardioides simplex Histamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe–4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 Å resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 Å. text/html Expression, purification, crystallization and preliminary X-ray studies of histamine dehydrogenase from Nocardioides simplex text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5311 Collagen prolyl-4-hydroxylase (C-P4H) catalyzes the hydroxylation of specific proline residues in procollagen, which is an essential step in collagen biosynthesis. A new form of P4H from Bacillus anthracis (anthrax-P4H) that shares many characteristics with the type I C-P4H from human has recently been characterized. The structure of anthrax-P4H could provide important insight into the chemistry of C-P4Hs and into the function of this unique homodimeric P4H. X-ray diffraction data of selenomethionine-labeled anthrax-P4H recombinantly expressed in Escherichia coli have been collected to 1.4 Å resolution. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Miller, M.A. Scott, E.E. Limburg, J. 2008-08-09 doi:10.1107/S1744309108023439 International Union of Crystallography Prolyl-4-hydroxylase from B. anthracis has been cloned, expressed and crystallized. A complete MAD data set has been collected to 1.4 Å resolution. en prolyl-4-hydroxylases Bacillus anthracis Collagen prolyl-4-hydroxylase (C-P4H) catalyzes the hydroxylation of specific proline residues in procollagen, which is an essential step in collagen biosynthesis. A new form of P4H from Bacillus anthracis (anthrax-P4H) that shares many characteristics with the type I C-P4H from human has recently been characterized. The structure of anthrax-P4H could provide important insight into the chemistry of C-P4Hs and into the function of this unique homodimeric P4H. X-ray diffraction data of selenomethionine-labeled anthrax-P4H recombinantly expressed in Escherichia coli have been collected to 1.4 Å resolution. text/html Expression, purification, crystallization and preliminary X-ray studies of a prolyl-4-hydroxylase protein from Bacillus anthracis text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?fw5184 YqjH is a cytoplasmic FAD-containing protein from Escherichia coli; based on homology to ViuB of Vibrio cholerae, it potentially acts as a ferri-siderophore reductase. This work describes its overexpression, purification, crystallization and structure solution at 3.0 Å resolution. YqjH shares high sequence similarity with a number of known siderophore-interacting proteins and its structure was solved by molecular replacement using the siderophore-interacting protein from Shewanella putrefaciens as the search model. The YqjH structure resembles those of other members of the NAD(P)H:flavin oxidoreductase superfamily. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Bamford, V.A. Armour, M. Mitchell, S.A. Cartron, M. Andrews, S.C. Watson, K.A. 2008-08-09 doi:10.1107/S174430910802352X International Union of Crystallography Crystallization of the proposed FAD-containing ferri-siderophore reductase protein YqjH from E. coli has been performed and the structure has been determined to 3.0 Å resolution. The structure shows similarity to another proposed siderophore-interacting protein from S. putrefaciens and weak similarity to members of the NAD(P)H:flavin oxidoreductase superfamily. en FAD iron reduction ViuB YqjH siderophores NAD(P)H:flavin oxidoreductases ferredoxin reductases YqjH is a cytoplasmic FAD-containing protein from Escherichia coli; based on homology to ViuB of Vibrio cholerae, it potentially acts as a ferri-siderophore reductase. This work describes its overexpression, purification, crystallization and structure solution at 3.0 Å resolution. YqjH shares high sequence similarity with a number of known siderophore-interacting proteins and its structure was solved by molecular replacement using the siderophore-interacting protein from Shewanella putrefaciens as the search model. The YqjH structure resembles those of other members of the NAD(P)H:flavin oxidoreductase superfamily. text/html Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?bw5256 Although LysR-type regulators (LTTRs) represent the largest family of transcriptional regulators in bacteria, the full-length structure of only one annotated LTTR (CbnR) has been deposited in the PDB. CrgA, a LTTR from pathogenic Neisseria meningitidis MC58, which is up-regulated upon bacterial cell contact with human epithelial cells, has been cloned, purified and crystallized. Crystals of full-length CrgA were obtained after buffer screening with a thermal shift assay and concentration with 0.2 M NDSB-256. Data were collected from two crystal forms of full-length CrgA belonging to space groups P212121 and P21, diffracting to 3.0 and 3.8 Å resolution and consistent with the presence of between six and ten and between ten and 20 copies of CrgA in the asymmetric unit, respectively. In addition, diffraction data were collected to 2.3 Å resolution from the selenomethionine derivative of the regulatory domain of CrgA. The crystals belonged to space group P21 and contained two molecules in the asymmetric unit. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Sainsbury, S. Ren, J. Saunders, N.J. Stuart, D.I. Owens, R.J. 2008-08-09 doi:10.1107/S1744309108024068 International Union of Crystallography The full length and the regulatory domain of the LysR-type transcriptional regulator CrgA have been crystallized. Diffraction data were collected from two crystal forms of full-length CrgA to 3.0 and 3.8 Å resolution, respectively. Crystals of the selenomethionine derivative of the C-terminal regulatory domain of CrgA diffracted to 2.3 Å resolution. en CrgA Neisseria meningitidis LysR-type regulators Although LysR-type regulators (LTTRs) represent the largest family of transcriptional regulators in bacteria, the full-length structure of only one annotated LTTR (CbnR) has been deposited in the PDB. CrgA, a LTTR from pathogenic Neisseria meningitidis MC58, which is up-regulated upon bacterial cell contact with human epithelial cells, has been cloned, purified and crystallized. Crystals of full-length CrgA were obtained after buffer screening with a thermal shift assay and concentration with 0.2 M NDSB-256. Data were collected from two crystal forms of full-length CrgA belonging to space groups P212121 and P21, diffracting to 3.0 and 3.8 Å resolution and consistent with the presence of between six and ten and between ten and 20 copies of CrgA in the asymmetric unit, respectively. In addition, diffraction data were collected to 2.3 Å resolution from the selenomethionine derivative of the regulatory domain of CrgA. The crystals belonged to space group P21 and contained two molecules in the asymmetric unit. text/html Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58 text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5157 Avian infectious bronchitis virus (IBV) encodes 15 nonstructural proteins (nsps) which play crucial roles in RNA transcription and genome replication. One of them, nsp3, contains an ADRP (adenosine diphosphate-ribose-1′-phosphatase) domain which was revealed in recent studies to have ADP-ribose-1′-monophosphatase (Appr-1′-pase) activity. Appr-1′-pase catalyzes the conversion of ADP-ribose-1′-monophosphate (Appr-1′-p) to ADP-ribose in the tRNA-splicing pathway. The gene segment encoding the IBV nsp3 ADRP domain has been cloned and expressed in Escherichia coli. The protein has been crystallized and the crystals diffracted to 1.8 Å resolution. They belonged to space group P1, with unit-cell parameters a = 41.1, b = 43.2, c = 48.9 Å, α = 78.0, β = 80.0, γ = 73.6°. Each asymmetric unit contains two molecules. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Wei, L. Chen, C. Zhao, Q. Li, C. Cong, L. Xu, X. Ma, Y. Liao, M. Xu, Y. Rao, Z. 2008-08-09 doi:10.1107/S1744309108024391 International Union of Crystallography The crystal of the nsp3 ADRP domain of avian infectious bronchitis virus (IBV) has been obtained and subjected to further crystallograghic studies. en avian infectious bronchitis virus nonstructural proteins ADRP domains Avian infectious bronchitis virus (IBV) encodes 15 nonstructural proteins (nsps) which play crucial roles in RNA transcription and genome replication. One of them, nsp3, contains an ADRP (adenosine diphosphate-ribose-1′-phosphatase) domain which was revealed in recent studies to have ADP-ribose-1′-monophosphatase (Appr-1′-pase) activity. Appr-1′-pase catalyzes the conversion of ADP-ribose-1′-monophosphate (Appr-1′-p) to ADP-ribose in the tRNA-splicing pathway. The gene segment encoding the IBV nsp3 ADRP domain has been cloned and expressed in Escherichia coli. The protein has been crystallized and the crystals diffracted to 1.8 Å resolution. They belonged to space group P1, with unit-cell parameters a = 41.1, b = 43.2, c = 48.9 Å, α = 78.0, β = 80.0, γ = 73.6°. Each asymmetric unit contains two molecules. text/html Purification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domain text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?pu5227 The gene product of open reading frame Rv1018c from Mycobacterium tuberculosis is annotated as encoding a probable N-acetylglucosamine 1-phosphate uridylyltransferase (MtbGlmU), an enzyme that catalyzes the biosynthesis of UDP-N-acetylglucosamine, a precursor common to lipopolysaccharide and peptidoglycan biosynthesis. Following overexpression in Escherichia coli, the enzyme was purified and crystallized using the hanging-drop vapour-diffusion method. Native diffraction data were collected from crystals belonging to space group R32 and processed to a resolution of 2.2 Å. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Yin, J. Garen, C.R. Cherney, M.M. Cherney, L.T. James, M.N.G. 2008-08-09 doi:10.1107/S1744309108024500 International Union of Crystallography N-Acetylglucosamine 1-phosphate uridyltransferase (GlmU) from M. tuberculosis H37Rv has been crystallized and preliminary X-ray crystallographic analysis has been performed. GlmU is a bi-domained bifunctional enzyme that is involved in the biosynthesis of UDP-N-acetylglucosamine, a precursor in peptidoglycan biosynthesis in M. tuberculosis. en Mycobacterium tuberculosis H37Rv Rv1018c N-acetylglucosamine 1-phosphate uridyltransferase peptidoglycan metabolism GlmU The gene product of open reading frame Rv1018c from Mycobacterium tuberculosis is annotated as encoding a probable N-acetylglucosamine 1-phosphate uridylyltransferase (MtbGlmU), an enzyme that catalyzes the biosynthesis of UDP-N-acetylglucosamine, a precursor common to lipopolysaccharide and peptidoglycan biosynthesis. Following overexpression in Escherichia coli, the enzyme was purified and crystallized using the hanging-drop vapour-diffusion method. Native diffraction data were collected from crystals belonging to space group R32 and processed to a resolution of 2.2 Å. text/html Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5312 Proteins with both peptidylprolyl isomerase (PPIase) and chaperone activities play a crucial role in protein folding in the periplasm of Gram-negative bacteria. Few such proteins have been structurally characterized and to date only the crystal structure of SurA from Escherichia coli has been reported. Par27, the prototype of a new group of parvulins, has recently been identified. Par27 exhibits both chaperone and PPIase activities in vitro and is the first identified parvulin protein that forms dimers in solution. Par27 has been expressed in E. coli. The protein was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Form A, which belongs to space group P2 (unit-cell parameters a = 42.2, b = 142.8, c = 56.0 Å, β = 95.1°), diffracts to 2.8 Å resolution, while form B, which belongs to space group C222 (unit-cell parameters a = 54.6, b = 214.1, c = 57.8 Å), diffracts to 2.2 Å resolution. Preliminary diffraction data analysis agreed with the presence of one monomer in the asymmetric unit of the orthorhombic crystal form and two in the monoclinic form. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Wohlkönig, A. Hodak, H. Clantin, B. Sénéchal, M. Bompard, C. Jacob-Dubuisson, F. Villeret, V. 2008-08-09 doi:10.1107/S1744309108024731 International Union of Crystallography Par27 from B. pertussis, the prototype of a new group of parvulins has been crystallized in two different crystal forms. en peptidylprolyl isomerases Par27 parvulins Bordetella pertussis Proteins with both peptidylprolyl isomerase (PPIase) and chaperone activities play a crucial role in protein folding in the periplasm of Gram-negative bacteria. Few such proteins have been structurally characterized and to date only the crystal structure of SurA from Escherichia coli has been reported. Par27, the prototype of a new group of parvulins, has recently been identified. Par27 exhibits both chaperone and PPIase activities in vitro and is the first identified parvulin protein that forms dimers in solution. Par27 has been expressed in E. coli. The protein was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Form A, which belongs to space group P2 (unit-cell parameters a = 42.2, b = 142.8, c = 56.0 Å, β = 95.1°), diffracts to 2.8 Å resolution, while form B, which belongs to space group C222 (unit-cell parameters a = 54.6, b = 214.1, c = 57.8 Å), diffracts to 2.2 Å resolution. Preliminary diffraction data analysis agreed with the presence of one monomer in the asymmetric unit of the orthorhombic crystal form and two in the monoclinic form. text/html Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussis text 9 64 2008-08-09 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5149 Fusarium head blight, one of the most destructive crop diseases, is mainly caused by Fusarium graminearum (known in its sexual stage as Gibberella zeae). F. graminearum secretes various extracellular enzymes that have been hypothesized to be involved in host infection. One of the extracellular enzymes secreted by this organism is the G. zeae extracellular lipase (GZEL), which is encoded by the FGL1 gene. In order to solve the crystal structure of GZEL and to gain a better understanding of the biological functions of the protein and of possible inhibitory mechanisms of lipase inhibitors, recombinant GZEL was crystallized at 291 K using PEG 3350 as a precipitant. A data set was collected to 2.8 Å resolution from a single flash-cooled crystal (100 K). The crystal belonged to space group P212121, with unit-cell parameters a = 78.4, b = 91.0, c = 195.8 Å, α = β = γ = 90°. The presence of four molecules was assumed per asymmetric unit, which gave a Matthews coefficient of 2.6 Å3 Da−1. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Sun, Y. Li, M. Zhang, Y. Liu, L. Liu, Y. Liu, Z. Li, X. Lou, Z. 2008-08-20 doi:10.1107/S1744309108019283 International Union of Crystallography G. zeae extracellular lipase has been overexpressed, purified and crystallized. Diffraction data were collected to 2.8 Å resolution. en extracellular lipases Fusarium graminearum Gibberella zeae fusarium head blight Fusarium head blight, one of the most destructive crop diseases, is mainly caused by Fusarium graminearum (known in its sexual stage as Gibberella zeae). F. graminearum secretes various extracellular enzymes that have been hypothesized to be involved in host infection. One of the extracellular enzymes secreted by this organism is the G. zeae extracellular lipase (GZEL), which is encoded by the FGL1 gene. In order to solve the crystal structure of GZEL and to gain a better understanding of the biological functions of the protein and of possible inhibitory mechanisms of lipase inhibitors, recombinant GZEL was crystallized at 291 K using PEG 3350 as a precipitant. A data set was collected to 2.8 Å resolution from a single flash-cooled crystal (100 K). The crystal belonged to space group P212121, with unit-cell parameters a = 78.4, b = 91.0, c = 195.8 Å, α = β = γ = 90°. The presence of four molecules was assumed per asymmetric unit, which gave a Matthews coefficient of 2.6 Å3 Da−1. text/html Crystallization and preliminary crystallographic analysis of Gibberella zeae extracellular lipase text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5304 Calcium ions play an important regulatory role in eukaryotes. However, the regulatory roles of Ca2+ in prokaryotes are poorly understood. CalD, an 18 kDa calcium-binding protein from the model actinomycete Streptomyces coelicolor A3(2), was purified and crystallized for structure determination by X-ray crystallography. Crystals of CalD that were suitable for X-ray diffraction were obtained using the hanging-drop vapour-diffusion method and diffraction data were collected in-house to 1.56 Å resolution. The crystals belonged to space group P212121, with unit-cell parameters a = 32.9, b = 51.0, c = 87.0 Å, α = β = γ = 90.0°. There is one protein molecule per asymmetric unit. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Zhao, X. Wang, S. Pang, H. Yang, K. Bartlam, M. 2008-08-20 doi:10.1107/S1744309108019891 International Union of Crystallography The calcium-binding protein encoded by the CalD gene in S. coelicolor A3(2) has been crystallized as a prelude towards the determination of its three-dimensional structure by X-ray crystallography. en CalD calcium-binding proteins Streptomyces coelicolor Calcium ions play an important regulatory role in eukaryotes. However, the regulatory roles of Ca2+ in prokaryotes are poorly understood. CalD, an 18 kDa calcium-binding protein from the model actinomycete Streptomyces coelicolor A3(2), was purified and crystallized for structure determination by X-ray crystallography. Crystals of CalD that were suitable for X-ray diffraction were obtained using the hanging-drop vapour-diffusion method and diffraction data were collected in-house to 1.56 Å resolution. The crystals belonged to space group P212121, with unit-cell parameters a = 32.9, b = 51.0, c = 87.0 Å, α = β = γ = 90.0°. There is one protein molecule per asymmetric unit. text/html Crystallization and preliminary X-ray diffraction studies of the calcium-binding protein CalD from Streptomyces coelicolor text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?gj5048 Proliferating cell nuclear antigen (PCNA) is an evolutionarily conserved protein that forms a ring-shaped homotrimer that functions as a sliding clamp for DNA replication. The rev6-1 mutation of Saccharomyces cerevisiae, which inactivates both translesion DNA synthesis and damage-avoidance pathways while having little effect on normal cell growth, has a G178S substitution in the PCNA protein. Human PCNA protein carrying the G178S substitution was crystallized. Two crystal forms were obtained under similar conditions. Crystal forms I and II belong to space groups P21, with unit-cell parameters a = 84.1, b = 130.2, c = 97.8 Å, β = 113.4°, and P212121, with unit-cell parameters a = 68.1, b = 100.2, c = 131.2 Å, respectively. Structural analyses by molecular replacement are now in progress. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Hishiki, A. Shimizu, T. Serizawa, A. Ohmori, H. Sato, M. Hashimoto, H. 2008-08-20 doi:10.1107/S174430910802277X International Union of Crystallography Crystallization and diffraction studies of human PCNA G178S mutant are reported. en PCNA DNA replication DNA damage tolerance translesion DNA synthesis Proliferating cell nuclear antigen (PCNA) is an evolutionarily conserved protein that forms a ring-shaped homotrimer that functions as a sliding clamp for DNA replication. The rev6-1 mutation of Saccharomyces cerevisiae, which inactivates both translesion DNA synthesis and damage-avoidance pathways while having little effect on normal cell growth, has a G178S substitution in the PCNA protein. Human PCNA protein carrying the G178S substitution was crystallized. Two crystal forms were obtained under similar conditions. Crystal forms I and II belong to space groups P21, with unit-cell parameters a = 84.1, b = 130.2, c = 97.8 Å, β = 113.4°, and P212121, with unit-cell parameters a = 68.1, b = 100.2, c = 131.2 Å, respectively. Structural analyses by molecular replacement are now in progress. text/html Crystallographic study of G178S mutant of human proliferating cell nuclear antigen text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?pu5229 Human DNA polymerase δ (Pol δ) consists of four subunits: p125, p50, p66 and p12. A heterodimer containing a His-tagged p50 subunit (p50) and a p50-interacting domain of the p66 subunit (p66N) was crystallized. The crystal was in the form of a prism with a rhombic cross-section and belonged to space group P21. The crystal had unit-cell parameters a = 95.13, b = 248.54, c = 103.46 Å, β = 106.94° and diffracted to a resolution of 3 Å. Four molecules of p50–p66N in an asymmetric unit corresponded to a crystal solvent content of 72.2%. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Baranovskiy, A.G. Babayeva, N.D. Pavlov, Y.I. Tahirov, T.H. 2008-08-20 doi:10.1107/S1744309108025086 International Union of Crystallography The cloning, expression, purification and crystallization of the complex of the second and third regulatory subunits of human Pol δ are reported. The crystals were characterized and an X-ray diffraction data set was collected to a resolution of 3 Å. en human DNA polymerase δ Pol δ p50 subunit p66 subunit Human DNA polymerase δ (Pol δ) consists of four subunits: p125, p50, p66 and p12. A heterodimer containing a His-tagged p50 subunit (p50) and a p50-interacting domain of the p66 subunit (p66N) was crystallized. The crystal was in the form of a prism with a rhombic cross-section and belonged to space group P21. The crystal had unit-cell parameters a = 95.13, b = 248.54, c = 103.46 Å, β = 106.94° and diffracted to a resolution of 3 Å. Four molecules of p50–p66N in an asymmetric unit corresponded to a crystal solvent content of 72.2%. text/html Crystallization and preliminary crystallographic analysis of the complex of the second and third regulatory subunits of human Pol δ text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5162 Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3121 or P3221, with unit-cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Jeong, B.-C. Yoo, K.S. Jung, K.W. Shin, J.S. Song, H.K. 2008-08-20 doi:10.1107/S1744309108025128 International Union of Crystallography Native and selenomethionine-derivatized CDCP2 from A. thaliana have been overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution. en Arabidopsis thaliana cystathionine β-synthase CBS domain CDCP2 Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3121 or P3221, with unit-cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%. text/html Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine β-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5152 The enzyme l-threonine dehydrogenase catalyses the NAD+-dependent conversion of l-threonine to 2-amino-3-ketobutyrate, which is the first reaction of a two-step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of l-threonine dehydrogenase (Tk-TDH) from the hyperthermophilic organism Thermococcus kodakaraensis KOD1 is reported. This threonine dehydrogenase consists of 350 amino acids, with a molecular weight of 38 kDa, and was prepared using an Escherichia coli expression system. The purified native protein was crystallized using the hanging-drop vapour-diffusion method and crystals grew in the tetragonal space group P43212, with unit-cell parameters a = b = 124.5, c = 271.1 Å. Diffraction data were collected to 2.6 Å resolution and preliminary analysis indicates that there are four molecules in the asymmetric unit of the crystal. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Bowyer, A. Mikolajek, H. Wright, J.N. Coker, A. Erskine, P.T. Cooper, J.B. Bashir, Q. Rashid, N. Jamil, F. Akhtar, M. 2008-08-20 doi:10.1107/S1744309108025384 International Union of Crystallography The l-threonine dehydrogenase from T. kodakaraensis KOD1 has been crystallized in the tetragonal space group P43212, with unit-cell parameters a = b = 124.5, c = 271.1 Å. Diffraction data were collected to 2.6 Å resolution and preliminary analysis indicates that there are four molecules in the crystallographic asymmetric unit. en l-threonine dehydrogenase thermophiles The enzyme l-threonine dehydrogenase catalyses the NAD+-dependent conversion of l-threonine to 2-amino-3-ketobutyrate, which is the first reaction of a two-step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of l-threonine dehydrogenase (Tk-TDH) from the hyperthermophilic organism Thermococcus kodakaraensis KOD1 is reported. This threonine dehydrogenase consists of 350 amino acids, with a molecular weight of 38 kDa, and was prepared using an Escherichia coli expression system. The purified native protein was crystallized using the hanging-drop vapour-diffusion method and crystals grew in the tetragonal space group P43212, with unit-cell parameters a = b = 124.5, c = 271.1 Å. Diffraction data were collected to 2.6 Å resolution and preliminary analysis indicates that there are four molecules in the asymmetric unit of the crystal. text/html Crystallization and preliminary X-ray diffraction analysis of l-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ll5163 Glutamate is the major excitatory neurotransmitter in the brain. Among the cognate ionotropic glutamate receptors, the subfamily selective for AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) is responsible for most fast excitatory synaptic signaling and plays key roles in synaptic plasticity. AMPA receptors (AMPA-Rs) have also been implicated in a number of neurological disorders. To investigate subunit-specific differences in the ligand binding and activation of AMPA-Rs, the GluR4 AMPA-R ligand-binding domain (LBD) was crystallized in complex with full and partial agonists. This is the first non-GluR2 AMPA-R LBD available for structural analysis. Standard cryoprotection protocols yielded high-resolution diffraction from flash-cooled crystals of the complex with the full agonist glutamate. However, for cocrystals with the partial agonist kainate, systematic screening and optimization of cryoprotection conditions yielded at best mosaic, weak diffraction at 100 K. In contrast, room-temperature data collection from capillary-mounted kainate cocrystals exhibited reproducible diffraction to better than 3 Å resolution. Together, these crystals lay the foundation for a structural comparison of LBD–agonist interactions in distinct AMPA-R subunits. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Gill, A. Madden, D.R. 2008-08-20 doi:10.1107/S1744309108025426 International Union of Crystallography High-resolution diffraction was obtained from GluR4 AMPA-receptor ligand-binding domain crystals using a combination of cryogenic and room-temperature data-collection strategies. en ionotropic glutamate receptor AMPA-receptor ion channel GluR4 ligand-binding domain recombinant expression metal-affinity chromatography capillary mounting Glutamate is the major excitatory neurotransmitter in the brain. Among the cognate ionotropic glutamate receptors, the subfamily selective for AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) is responsible for most fast excitatory synaptic signaling and plays key roles in synaptic plasticity. AMPA receptors (AMPA-Rs) have also been implicated in a number of neurological disorders. To investigate subunit-specific differences in the ligand binding and activation of AMPA-Rs, the GluR4 AMPA-R ligand-binding domain (LBD) was crystallized in complex with full and partial agonists. This is the first non-GluR2 AMPA-R LBD available for structural analysis. Standard cryoprotection protocols yielded high-resolution diffraction from flash-cooled crystals of the complex with the full agonist glutamate. However, for cocrystals with the partial agonist kainate, systematic screening and optimization of cryoprotection conditions yielded at best mosaic, weak diffraction at 100 K. In contrast, room-temperature data collection from capillary-mounted kainate cocrystals exhibited reproducible diffraction to better than 3 Å resolution. Together, these crystals lay the foundation for a structural comparison of LBD–agonist interactions in distinct AMPA-R subunits. text/html Purification and crystallization of a non-GluR2 AMPA-receptor ligand-binding domain: a case of cryo-incompatibility addressed by room-temperature data collection text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?be5111 Over the last decade, protein purification has become more efficient and standardized through the introduction of affinity tags. The choice and position of the tag, however, can directly influence the process of protein crystallization. Octopine dehydrogenase (OcDH) without a His tag and tagged protein constructs such as OcDH-His5 and OcDH-LEHis6 have been investigated for their crystallizability. Only OcDH-His5 yielded crystals; however, they were multiple. To improve crystal quality, the cofactor NADH was added, resulting in single crystals that were suitable for structure determination. As shown by the structure, the His5 tag protrudes into the cleft between the NADH and l-arginine-binding domains and is mainly fixed in place by water molecules. The protein is thereby stabilized to such an extent that the formation of crystal contacts can proceed. Together with NADH, the His5 tag obviously locks the enzyme into a specific conformation which induces crystal growth. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Smits, S.H.J. Mueller, A. Grieshaber, M.K. Schmitt, L. 2008-08-20 doi:10.1107/S1744309108025487 International Union of Crystallography The crystal structure of octopine dehydrogenase revealed a specific role of the His5 tag in inducing the crystal contacts required for successful crystallization. en His tags coenzymes octopine crystal contacts Over the last decade, protein purification has become more efficient and standardized through the introduction of affinity tags. The choice and position of the tag, however, can directly influence the process of protein crystallization. Octopine dehydrogenase (OcDH) without a His tag and tagged protein constructs such as OcDH-His5 and OcDH-LEHis6 have been investigated for their crystallizability. Only OcDH-His5 yielded crystals; however, they were multiple. To improve crystal quality, the cofactor NADH was added, resulting in single crystals that were suitable for structure determination. As shown by the structure, the His5 tag protrudes into the cleft between the NADH and l-arginine-binding domains and is mainly fixed in place by water molecules. The protein is thereby stabilized to such an extent that the formation of crystal contacts can proceed. Together with NADH, the His5 tag obviously locks the enzyme into a specific conformation which induces crystal growth. text/html Coenzyme- and His-tag-induced crystallization of octopine dehydrogenase text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5314 The complex of RuvBL1 and its homologue RuvBL2, two evolutionarily highly conserved eukaryotic proteins belonging to the AAA+ (ATPase associated with diverse cellular activities) family of ATPases, was co-expressed in Escherichia coli. For crystallization purposes, the flexible domains II of RuvBL1 and RuvBL2 were truncated. The truncated RuvBL1–RuvBL2 complex was crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals were hexagonal-shaped plates and belonged to either the orthorhombic space group C2221, with unit-cell parameters a = 111.4, b = 188.0, c = 243.4 Å and six monomers in the asymmetric unit, or the monoclinic space group P21, with unit-cell parameters a = 109.2, b = 243.4, c = 109.3 Å, β = 118.7° and 12 monomers in the asymmetric unit. The crystal structure could be solved by molecular replacement in both possible space groups and the solutions obtained showed that the complex forms a dodecamer. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Gorynia, S. Matias, P.M. Bandeiras, T.M. Donner, P. Carrondo, M.A. 2008-08-20 doi:10.1107/S174430910802558X International Union of Crystallography A truncated variant of the human RuvBL1–RuvBL2 complex was cloned, expressed, purified and crystallised. Synchrotron diffraction data to 4 Å resolution were used to carry out a preliminary crystallographic analysis of the complex. en RuvBL1 RuvBL2 ATPases The complex of RuvBL1 and its homologue RuvBL2, two evolutionarily highly conserved eukaryotic proteins belonging to the AAA+ (ATPase associated with diverse cellular activities) family of ATPases, was co-expressed in Escherichia coli. For crystallization purposes, the flexible domains II of RuvBL1 and RuvBL2 were truncated. The truncated RuvBL1–RuvBL2 complex was crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals were hexagonal-shaped plates and belonged to either the orthorhombic space group C2221, with unit-cell parameters a = 111.4, b = 188.0, c = 243.4 Å and six monomers in the asymmetric unit, or the monoclinic space group P21, with unit-cell parameters a = 109.2, b = 243.4, c = 109.3 Å, β = 118.7° and 12 monomers in the asymmetric unit. The crystal structure could be solved by molecular replacement in both possible space groups and the solutions obtained showed that the complex forms a dodecamer. text/html Cloning, expression, purification, crystallization and preliminary X-ray analysis of the human RuvBL1–RuvBL2 complex text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5315 A non-Pfam hypothetical protein SCO4226 of molecular weight 9 kDa from Streptomyces coelicolor A3(2) was overexpressed in Escherichia coli and the purified recombinant protein was crystallized using the sitting-drop vapour-diffusion method. An X-ray diffraction data set was collected to 2.0 Å resolution. The crystal belonged to space group P21, with unit-cell parameters a = 29.67, b = 67.00, c = 34.43 Å, α = γ = 90.00, β = 94.26°. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Wang, S. He, Y.-X. Bao, R. Teng, Y.-B. Ye, B.-P. Zhou, C.-Z. 2008-08-20 doi:10.1107/S174430910802575X International Union of Crystallography A hypothetical protein SCO4226 from S. coelicolor has been overexpressed, purified and crystallized. The crystals belonged to space group P21 and diffracted to 2.0 Å resolution. en SCO4226 Streptomyces coelicolor A non-Pfam hypothetical protein SCO4226 of molecular weight 9 kDa from Streptomyces coelicolor A3(2) was overexpressed in Escherichia coli and the purified recombinant protein was crystallized using the sitting-drop vapour-diffusion method. An X-ray diffraction data set was collected to 2.0 Å resolution. The crystal belonged to space group P21, with unit-cell parameters a = 29.67, b = 67.00, c = 34.43 Å, α = γ = 90.00, β = 94.26°. text/html Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SCO4226 from Streptomyces coelicolor A3(2) text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?bo5046 Flavoredoxin from Desulfovibrio vulgaris Miyazaki F has been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with 10%(w/v) PEG 8000, 0.2 M zinc acetate and 100 mM MES pH 6.0. The diffraction pattern of the crystal extended to 1.05 Å resolution under cryogenic conditions. The space group was determined to be P3121, with unit-cell parameters a = b = 53.35, c = 116.22 Å. Phase determination was carried out by the SAD method using methylmercuric chloride. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Ueda, Y. Shibata, N. Takeuchi, D. Kitamura, M. Higuchi, Y. 2008-08-20 doi:10.1107/S1744309108025840 International Union of Crystallography Flavoredoxin from D. vulgaris Miyazaki F has been purified and crystallized. The crystals diffracted to 1.05 Å resolution using synchrotron radiation. en flavoredoxins sulfate-reducing bacteria electron transfer Flavoredoxin from Desulfovibrio vulgaris Miyazaki F has been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with 10%(w/v) PEG 8000, 0.2 M zinc acetate and 100 mM MES pH 6.0. The diffraction pattern of the crystal extended to 1.05 Å resolution under cryogenic conditions. The space group was determined to be P3121, with unit-cell parameters a = b = 53.35, c = 116.22 Å. Phase determination was carried out by the SAD method using methylmercuric chloride. text/html Crystallization and preliminary X-ray crystallographic study of flavoredoxin from Desulfovibrio vulgaris Miyazaki F text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?bo5045 The 716-amino-acid guanidino kinase from the parasitic flatworm Schistosoma mansoni results from the fusion of two guanidino kinase subunits. Crystals of this 80 kDa protein have been obtained in the monoclinic space group P21, with unit-cell parameters a = 52.7, b = 122.1, c = 63.2 Å, β = 108.5°. Synchrotron data were collected to 2.8 Å resolution on ESRF beamline ID29. The structure was solved by the molecular-replacement method, using the 357-amino-acid structure of the arginine kinase from Trypanosoma cruzi as the search model. Copyright (c) 2008 International Union of Crystallography urn:issn:1744-3091 Awama, A.M. Paracuellos, P. Laurent, S. Dissous, C. Marcillat, O. Gouet, P. 2008-08-20 doi:10.1107/S1744309108025979 International Union of Crystallography The X-ray structure of the guanidino kinase from S. mansoni has been determined at 2.8 Å resolution by the molecular-replacement method. en guanidino kinase Schistosoma mansoni The 716-amino-acid guanidino kinase from the parasitic flatworm Schistosoma mansoni results from the fusion of two guanidino kinase subunits. Crystals of this 80 kDa protein have been obtained in the monoclinic space group P21, with unit-cell parameters a = 52.7, b = 122.1, c = 63.2 Å, β = 108.5°. Synchrotron data were collected to 2.8 Å resolution on ESRF beamline ID29. The structure was solved by the molecular-replacement method, using the 357-amino-acid structure of the arginine kinase from Trypanosoma cruzi as the search model. text/html Crystallization and X-ray analysis of the Schistosoma mansoni guanidino kinase text 9 64 2008-08-20 Copyright (c) 2008 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0