Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 7 (July 2005)



[Issue Author Index][Volume Author Index]
[Cover illustration] Cover illustration: The protein product of the At2g17340 gene from Arabidopsis thaliana (p. 630).

protein structure communications


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Acta Cryst. (2005). F61, 621-624  [ doi:10.1107/S1744309105017380 ]

Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre

I. W. Boucher, A. K. Kalliomaa, V. M. Levdikov, E. V. Blagova, M. J. Fogg, J. A. Brannigan, K. S. Wilson and A. J. Wilkinson

Synopsis: The crystal structures of two manganese superoxide dismutases from B. anthracis were solved by X-ray crystallography using molecular replacement.

PDB references: 1xuq and 1xre

Online 15 June 2005


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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 diphosphate

T. Sgraja, L. E. Kemp, N. Ramsden and W. N. Hunter

Synopsis: 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


structural genomics communications


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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 thaliana

E. Bitto, C. A. Bingman, S. T. M. Allard, G. E. Wesenberg and G. N. Phillips

Synopsis: 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


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Acta Cryst. (2005). F61, 636-639  [ doi:10.1107/S1744309105019263 ]

The first crystal structure of an archaeal helical repeat protein

K. Yoneda, H. Sakuraba, H. Tsuge, N. Katunuma, S. Kuramitsu, T. Kawabata and T. Ohshima

Synopsis: 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


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Acta Cryst. (2005). F61, 640-646  [ doi:10.1107/S1744309105019780 ]

Structure of a NAD kinase from Thermotoga maritima at 2.3 Å resolution

V. Oganesyan, C. Huang, P. D. Adams, J. Jancarik, H. A. Yokota, R. Kim and S.-H. Kim

Synopsis: 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


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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 thaliana

S. T. M. Allard, C. A. Bingman, K. A. Johnson, G. E. Wesenberg, E. Bitto, W. B. Jeon and G. N. Phillips

Synopsis: 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


crystallization communications


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Acta Cryst. (2005). F61, 651-654  [ doi:10.1107/S1744309105016933 ]

Crystallization of the C-terminal globular domain of avian reovirus fibre

M. J. van Raaij, X. L. Hermo Parrado, P. Guardado Calvo, G. C. Fox, A. L. Llamas-Saiz, C. Costas, J. Martínez-Costas and J. Benavente

Synopsis: Partial proteolysis of the avian reovirus cell-attachment protein [sigma]C yields a major homotrimeric C-terminal fragment that presumably contains the receptor-binding domain. This fragment has been crystallized in the presence and absence of zinc sulfate and cadmium sulfate. One of the crystal forms diffracts synchrotron X-rays to 2.2-2.3 Å.

Online 15 June 2005


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Acta Cryst. (2005). F61, 655-658  [ doi:10.1107/S1744309105016969 ]

Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbA

C. L. Reyes and G. Chang

Synopsis: 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


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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 peroxiredoxin

J. Choi, S. Choi, J. Choi, M.-K. Cha, I.-H. Kim and W. Shin

Synopsis: 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


 

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Acta Cryst. (2005). F61, 663-665  [ doi:10.1107/S1744309105017458 ]

Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase

Y. Xu, D. Wen, C. Brown, C.-J. Chen, P. D. Carr, D. L. Ollis and S. G. Vasudevan

Synopsis: 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


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Acta Cryst. (2005). F61, 666-668  [ doi:10.1107/S1744309105017392 ]

Crystallization and X-ray crystallographic analysis of human STAT1

X. Mao and X. Chen

Synopsis: 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


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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 system

K. Lee, R. Friemann, J. V. Parales, D. T. Gibson and S. Ramaswamy

Synopsis: All three components of the toluene dioxygenase system have been expressed, purified and crystallized.

Online 15 June 2005


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Acta Cryst. (2005). F61, 673-675  [ doi:10.1107/S1744309105018014 ]

Purification, crystallization and preliminary X-ray diffraction studies on human Ca2+-binding protein S100B

T. Ostendorp, C. W. Heizmann, P. M. H. Kroneck and G. Fritz

Synopsis: 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


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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 campestris

D. Shi, X. Yu, L. Roth, H. Morizono, Y. Hathout, N. M. Allewell and M. Tuchman

Synopsis: 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


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Acta Cryst. (2005). F61, 680-683  [ doi:10.1107/S1744309105017987 ]

Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis

P. Rathinaswamy, A. V. Pundle, A. A. Prabhune, H. SivaRaman, J. A. Brannigan, G. G. Dodson and C. G. Suresh

Synopsis: 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


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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-diffusion

C. Biertümpfel, J. Basquin, R. P. Birkenbihl, D. Suck and C. Sauter

Synopsis: 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


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Acta Cryst. (2005). F61, 688-690  [ doi:10.1107/S1744309105018427 ]

Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)[alpha]-hydroxysteroid dehydrogenase

O. El-Kabbani, S. Ishikura, A. Wagner, C. Schulze-Briese and A. Hara

Synopsis: Orthorhombic crystals of mouse 3(17)[alpha]-hydroxysteroid dehydrogenase were obtained from buffered polyethylene glycol solutions. The crystals diffracted to a resolution of 1.8 Å at the Swiss Light Source beamline X06SA.

Online 23 June 2005


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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 campestris

K.-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. Chou

Synopsis: 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


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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 campestris

K.-H. Chin, W.-T. Kuo, C.-C. Chou, H.-L. Shr, P.-C. Lyu, A.H.-J. Wang and S.-H. Chou

Synopsis: 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


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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 analysis

C.-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. Chou

Synopsis: 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


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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 campestris

K.-H. Chin, C.-C. Chou, C.-C. Lee, H.-L. Shr, P.-C. Lyu, A.H.-J. Wang and S.-H. Chou

Synopsis: 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


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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 campestris

C.-Y. Yang, K.-H. Chin, C.-C. Chou, H.-L. Shr, F. P. Gao, P.-C. Lyu, A.H.-J. Wang and S.-H. Chou

Synopsis: 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


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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 campestris

Z.-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. Chou

Synopsis: 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


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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 antibiotics

E. Nango, T. Kumasaka, T. Sato, N. Tanaka, K. Kakinuma and T. Eguchi

Synopsis: 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


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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 biosynthesis

J. Harada, K. Wada, H. Yamaguchi, H. Oh-oka, H. Tamiaki and K. Fukuyama

Synopsis: 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


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Acta Cryst. (2005). F61, 715-717  [ doi:10.1107/S1744309105019251 ]

X-ray diffraction analysis of a crystal of HscA from Escherichia coli

P. C. Aoto, D. T. Ta, J. R. Cupp-Vickery and L. E. Vickery

Synopsis: 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


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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 tuberculosis

G. Kefala, R. Janowski, S. Panjikar, C. Mueller-Dieckmann and M. S. Weiss

Synopsis: 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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