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Cover illustration: The protein product of the At2g17340 gene from Arabidopsis thaliana (p. 630). |
Acta Cryst. (2005). F61, 621-624 [ doi:10.1107/S1744309105017380 ] Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centreI. W. Boucher, A. K. Kalliomaa, V. M. Levdikov, E. V. Blagova, M. J. Fogg, J. A. Brannigan, K. S. Wilson and A. J. WilkinsonSynopsis: The crystal structures of two manganese superoxide dismutases from B. anthracis were solved by X-ray crystallography using molecular replacement. Online 15 June 2005 |
Acta Cryst. (2005). F61, 625-629 [ doi:10.1107/S1744309105018762 ] A double mutation of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphateT. Sgraja, L. E. Kemp, N. Ramsden and W. N. HunterSynopsis: A double mutation designed to disrupt binding of isoprenoid diphosphate to an enzyme involved in isoprenoid biosynthesis was made and the structure determined. Despite the removal of six hydrogen-bonding interactions, the ligand, acquired during production in E. coli, remains bound. The reasons for this are discussed. PDB reference: 1yqn Online 30 June 2005 |
Acta Cryst. (2005). F61, 630-635 [ doi:10.1107/S1744309105017690 ] The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thalianaE. Bitto, C. A. Bingman, S. T. M. Allard, G. E. Wesenberg and G. N. PhillipsSynopsis: The crystal structure of the 40.8 kDa At2g17340 protein from A. thaliana was determined at 1.7 Å resolution. The structure provides the first insight into the structural organization of the Pfam01937.11 family and establishes that the proteins of this family coordinate a metal in its putative active site. PDB reference: 1xfi Online 23 June 2005 |
Acta Cryst. (2005). F61, 636-639 [ doi:10.1107/S1744309105019263 ] The first crystal structure of an archaeal helical repeat proteinK. Yoneda, H. Sakuraba, H. Tsuge, N. Katunuma, S. Kuramitsu, T. Kawabata and T. OhshimaSynopsis: The crystal structure of ST1625p, a protein encoded by a hypothetical open reading frame ST1625 in the genome of the hyperthermophilic archaeon Sulfolobus tokodaii, was determined at 2.2 Å resolution. The structure of ST1625p consists of a unique superhelix with a low-level structure resemblance to doamins from other proteins with known three-dimensional structures. PDB reference: 1wy6 Online 30 June 2005 |
Acta Cryst. (2005). F61, 640-646 [ doi:10.1107/S1744309105019780 ] Structure of a NAD kinase from Thermotoga maritima at 2.3 Å resolutionV. Oganesyan, C. Huang, P. D. Adams, J. Jancarik, H. A. Yokota, R. Kim and S.-H. KimSynopsis: The expression, purification, crystallization, and structure determination of NAD-kinase from T. maritima are reported. Similarity to other NAD-kinases as well as homo-oligomrization state of the enzyme from T. maritima are discussed. PDB reference: 1yt5 Online 30 June 2005 |
Acta Cryst. (2005). F61, 647-650 [ doi:10.1107/S1744309105019743 ] Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thalianaS. T. M. Allard, C. A. Bingman, K. A. Johnson, G. E. Wesenberg, E. Bitto, W. B. Jeon and G. N. PhillipsSynopsis: The crystal structure of the 18 kDa At3g22680 gene product from A. thaliana was determined at 1.6 Å resolution. At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformational space. PDB reference: 1vk5 Online 30 June 2005 |
Acta Cryst. (2005). F61, 651-654 [ doi:10.1107/S1744309105016933 ] Crystallization of the C-terminal globular domain of avian reovirus fibreM. J. van Raaij, X. L. Hermo Parrado, P. Guardado Calvo, G. C. Fox, A. L. Llamas-Saiz, C. Costas, J. Martínez-Costas and J. BenaventeSynopsis: Partial proteolysis of the avian reovirus cell-attachment protein Online 15 June 2005 |
Acta Cryst. (2005). F61, 655-658 [ doi:10.1107/S1744309105016969 ] Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbAC. L. Reyes and G. ChangSynopsis: The use of lipopolysaccharide in the crystallization of the integral membrane protein MsbA was critical to the overall stability of the crystals and led to an increase in diffraction resolution. Online 15 June 2005 |
Acta Cryst. (2005). F61, 659-662 [ doi:10.1107/S1744309105016970 ] Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxinJ. Choi, S. Choi, J. Choi, M.-K. Cha, I.-H. Kim and W. ShinSynopsis: A double mutant of yeast nuclear thiol peroxidase has been crystallized in a truncated form. The crystal belongs to space group P32, with unit-cell parameters a = b = 37.54, c = 83.26 Å. A diffraction data set has been collected to 1.8 Å resolution. Online 15 June 2005 |
Acta Cryst. (2005). F61, 663-665 [ doi:10.1107/S1744309105017458 ] Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferaseY. Xu, D. Wen, C. Brown, C.-J. Chen, P. D. Carr, D. L. Ollis and S. G. VasudevanSynopsis: The C-terminal domain of adenylyltransferase (ATase) from Escherichia coli has been overexpressed, purified and crystallized in a form suitable for structure analysis. Online 15 June 2005 |
Acta Cryst. (2005). F61, 666-668 [ doi:10.1107/S1744309105017392 ] Crystallization and X-ray crystallographic analysis of human STAT1X. Mao and X. ChenSynopsis: Human STAT1 (1-683) has been crystallized in the presence of a receptor-derived phosphopeptide. A diffraction data set has been collected and processed to 3.0 Å resolution. Online 15 June 2005 |
Acta Cryst. (2005). F61, 669-672 [ doi:10.1107/S1744309105017549 ] Purification, crystallization and preliminary X-ray diffraction studies of the three components of the toluene 2,3-dioxygenase enzyme systemK. Lee, R. Friemann, J. V. Parales, D. T. Gibson and S. RamaswamySynopsis: All three components of the toluene dioxygenase system have been expressed, purified and crystallized. Online 15 June 2005 |
Acta Cryst. (2005). F61, 673-675 [ doi:10.1107/S1744309105018014 ] Purification, crystallization and preliminary X-ray diffraction studies on human Ca2+-binding protein S100BT. Ostendorp, C. W. Heizmann, P. M. H. Kroneck and G. FritzSynopsis: Human recombinant EF-hand Ca2+-binding protein S100B has been purified and crystallized. A complete data set was recorded to 1.9 Å. Online 15 June 2005 |
Acta Cryst. (2005). F61, 676-679 [ doi:10.1107/S1744309105018051 ] Expression, purification, crystallization and preliminary X-ray crystallographic studies of a novel acetylcitrulline deacetylase from Xanthomonas campestrisD. Shi, X. Yu, L. Roth, H. Morizono, Y. Hathout, N. M. Allewell and M. TuchmanSynopsis: The expression, purification and preliminary X-ray diffraction studies of a novel N-acetyl-L-citrulline deacetylase from X. campestris are reported. Online 15 June 2005 |
Acta Cryst. (2005). F61, 680-683 [ doi:10.1107/S1744309105017987 ] Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilisP. Rathinaswamy, A. V. Pundle, A. A. Prabhune, H. SivaRaman, J. A. Brannigan, G. G. Dodson and C. G. SureshSynopsis: An unannotated protein reported from B. subtilis has been expressed in E. coli and identified as possessing penicillin V acylase activity. The crystallization and preliminary crystallographic analysis of this penicillin V acylase is presented. Online 15 June 2005 |
Acta Cryst. (2005). F61, 684-687 [ doi:10.1107/S1744309105018269 ] Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusionC. Biertümpfel, J. Basquin, R. P. Birkenbihl, D. Suck and C. SauterSynopsis: The Holliday junction-cutting enzyme Hjc from A. fulgidus was crystallized by the counter-diffusion method in agarose gel and complete data were collected at 2.7 Å resolution using synchrotron radiation. Online 15 June 2005 |
Acta Cryst. (2005). F61, 688-690 [ doi:10.1107/S1744309105018427 ] Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)
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Acta Cryst. (2005). F61, 691-693 [ doi:10.1107/S1744309105018798 ] Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestrisK.-H. Chin, Z.-W. Huang, K.-C. Wei, C.-C. Chou, C.-C. Lee, H.-L. Shr, F. P. Gao, P.-C. Lyu, A.H.-J. Wang and S.-H. ChouSynopsis: A conserved hypothetical protein XC1692 from X. campestris pv. campestris has been overexpressed in E. coli. The purified recombinant protein crystallized in a variety of forms and diffracted to a resolution of at least 1.45 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 694-696 [ doi:10.1107/S1744309105018944 ] Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestrisK.-H. Chin, W.-T. Kuo, C.-C. Chou, H.-L. Shr, P.-C. Lyu, A.H.-J. Wang and S.-H. ChouSynopsis: A conserved hypothetical protein XC229 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. A crystal of the purified recombinant protein diffracted to a resolution of 1.80 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 697-699 [ doi:10.1107/S1744309105018968 ] A putative polyketide-synthesis protein XC5357 from Xanthomonas campestris: heterologous expression, crystallization and preliminary X-ray analysisC.-L. Chu, K.-H. Chin, F.-Y. Lin, C.-C. Chou, C.-C. Lee, H.-L. Shr, P.-C. Lyu, A.H.-J. Wang and S.-H. ChouSynopsis: A putative polyketide-synthesis protein XC5357 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted to a resolution of at least 1.85 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 700-702 [ doi:10.1107/S1744309105018956 ] Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestrisK.-H. Chin, C.-C. Chou, C.-C. Lee, H.-L. Shr, P.-C. Lyu, A.H.-J. Wang and S.-H. ChouSynopsis: A putative ApaG gene product from X. campestris pv. campestris was overexpressed in E. coli, purified and crystallized. The crystals diffracted to a resolution of at least 2.3 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 703-705 [ doi:10.1107/S1744309105019391 ] Cloning, purification crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC6422 from Xanthomonas campestrisC.-Y. Yang, K.-H. Chin, C.-C. Chou, H.-L. Shr, F. P. Gao, P.-C. Lyu, A.H.-J. Wang and S.-H. ChouSynopsis: A conserved hypothetical protein XC6422 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. Crystals obtained from the purified recombinant protein showed a variety of forms that diffracted to at least 1.6 Å resolution. Online 30 June 2005 |
Acta Cryst. (2005). F61, 706-708 [ doi:10.1107/S1744309105019548 ] Cloning, expression, crystallization and preliminary X-ray analysis of a putative multiple antibiotic resistance repressor protein (MarR) from Xanthomonas campestrisZ.-L. Tu, J.-N. Li, K.-H. Chin, C.-C. Chou, C.-C. Lee, H.-L. Shr, P.-C. Lyu, F. P. Gao, A.H.-J. Wang and S.-H. ChouSynopsis: A putative repressor for the multiple antibiotic resistance operon from a plant pathogen X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted to 2.3 Å with good quality. Online 30 June 2005 |
Acta Cryst. (2005). F61, 709-711 [ doi:10.1107/S1744309105018841 ] Crystallization and X-ray analysis of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibioticsE. Nango, T. Kumasaka, T. Sato, N. Tanaka, K. Kakinuma and T. EguchiSynopsis: The crystallization of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics, is reported. Online 30 June 2005 |
Acta Cryst. (2005). F61, 712-714 [ doi:10.1107/S1744309105019093 ] Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesisJ. Harada, K. Wada, H. Yamaguchi, H. Oh-oka, H. Tamiaki and K. FukuyamaSynopsis: Recombinant BchU from C. tepidum has been crystallized. Crystals diffract to 2.27 Å using synchrotron radiation at SPring-8 and belong to space group P6122 or P6522, with unit-cell parameters a = b = 81.5, c = 250.7 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 715-717 [ doi:10.1107/S1744309105019251 ] X-ray diffraction analysis of a crystal of HscA from Escherichia coliP. C. Aoto, D. T. Ta, J. R. Cupp-Vickery and L. E. VickerySynopsis: A truncated form of HscA (52 kDa) containing both nucleotide- and substrate-binding domains has been crystallized and analyzed by X-ray diffraction. The crystal belongs to space group P212121 and diffracts to 2.9 Å. Online 30 June 2005 |
Acta Cryst. (2005). F61, 718-721 [ doi:10.1107/S174430910501938X ] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosisG. Kefala, R. Janowski, S. Panjikar, C. Mueller-Dieckmann and M. S. WeissSynopsis: M. tuberculosis dihydrodipicolinate reductase, the enzyme that catalyzes the second committed step of lysine biosynthesis, has been cloned, expressed, purified and crystallized in three different crystal forms. Online 30 June 2005 |
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