Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 62, Part 10 (October 2006)



[Issue Author Index][Volume Author Index]
[Cover illustration] Cover illustration: The first structure of a microbial aspartokinase, that from Methanococcus jannaschii, determined in the presence of the amino-acid substrate L-aspartic acid and the nucleotide product MgADP (p. 962).

protein structure communications


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Acta Cryst. (2006). F62, 944-948  [ doi:10.1107/S1744309106034075 ]

Structure of the heterotrimeric PCNA from Sulfolobus solfataricus

G. J. Williams, K. Johnson, J. Rudolf, S. A. McMahon, L. Carter, M. Oke, H. Liu, G. L. Taylor, M. F. White and J. H. Naismith

Synopsis: The structure of the heterotrimeric PCNA complex from S. sulfataricus is reported to 2.3 Å.

PDB reference: 2ix2

Online 19 September 2006


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Acta Cryst. (2006). F62, 949-953  [ doi:10.1107/S174430910603613X ]

Structure of Staphylococcus aureus guanylate monophosphate kinase

K. El Omari, B. Dhaliwal, M. Lockyer, I. Charles, A. R. Hawkins and D. K. Stammers

Synopsis: The crystal structure of S. aureus guanylate monophosphate kinase has been determined to 1.9 Å resolution, revealing both open and closed forms within the asymmetric unit. These structures may be of use in anti-bacterial drug design.

PDB reference: 2j41

Online 19 September 2006


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Acta Cryst. (2006). F62, 954-957  [ doi:10.1107/S1744309106036578 ]

Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima

A. V. Lyashenko, N. E. Zhukhlistova, A. G. Gabdoulkhakov, Y. N. Zhukova, W. Voelter, V. N. Zaitsev, I. Bento, E. V. Stepanova, G. S. Kachalova, O. V. Koroleva, E. A. Cherkashyn, V. I. Tishkov, V. S. Lamzin, K. Schirwitz, E. Y. Morgunova, C. Betzel, P. F. Lindley and A. M. Mikhailov

Synopsis: The crystallization and preliminary X-ray structure at 1.9 Å resolution of the fungal laccase from C. maxima are presented.

PDB reference: 2h5u

Online 19 September 2006


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Acta Cryst. (2006). F62, 958-961  [ doi:10.1107/S1744309106038164 ]

Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family

M. D. Costabel, M. R. Ermácora, J. A. Santomé, P. M. Alzari and D. M. A. Guérin

Synopsis: The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved.

PDB reference: 2fdq

Online 30 September 2006


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Acta Cryst. (2006). F62, 962-966  [ doi:10.1107/S1744309106038279 ]

The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase

C. R. Faehnle, X. Liu, A. Pavlovsky and R. E. Viola

Synopsis: The first structure of a microbial aspartokinase reveals details of its quaternary structure and the mode of substrate binding and provides insights into the catalytic mechanism.

PDB reference: 2hmf

Online 30 September 2006


crystallization communications


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Acta Cryst. (2006). F62, 967-969  [ doi:10.1107/S174430910603199X ]

Preparation, crystallization and preliminary X-ray analysis of protein YtlP from Bacillus subtilis

C. Liu, D. Li, L. Hederstedt, L. Li, Y.-H. Liang and X.-D. Su

Synopsis: The crystallization and preliminary X-ray crystallographic analysis of protein YtlP from B. subtilis is reported.

Online 19 September 2006


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Acta Cryst. (2006). F62, 970-972  [ doi:10.1107/S1744309106032982 ]

Crystallization and preliminary X-ray diffraction analysis of two extracytoplasmic solute receptors of the DctP family from Bordetella pertussis

P. Rucktooa, I. Huvent, R. Antoine, S. Lecher, F. Jacob-Dubuisson, V. Villeret and C. Bompard

Synopsis: Sample preparation, crystallization and preliminary X-ray analysis are reported for two B. pertussis extracytoplasmic solute receptors.

Online 19 September 2006


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Acta Cryst. (2006). F62, 973-975  [ doi:10.1107/S1744309106033100 ]

Crystallization and preliminary X-ray analysis of Salmonella FliI, the ATPase component of the type III flagellar protein-export apparatus

T. Minamino, K. Imada, A. Tahara, M. Kihara, R. M. Macnab and K. Namba

Synopsis: Crystals of an N-terminally truncated variant of the Salmonella flagellar ATPase FliI, which exports substrate proteins into the central channel of the growing flagellar structure by utilizing the energy of ATP hydrolysis, have been obtained and characterized by X-ray diffraction.

Online 19 September 2006


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Acta Cryst. (2006). F62, 976-979  [ doi:10.1107/S1744309106033537 ]

Crystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major

D. Bisacchi, Y. Zhou, B. P. Rosen, R. Mukhopadhyay and D. Bordo

Synopsis: LmACR2 from L. major is the first rhodanese-like enzyme directly involved in the reduction of arsenate and antimonate to be crystallized. Diffraction data have been collected to 1.99 Å resolution using synchrotron X-rays.

Online 19 September 2006


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Acta Cryst. (2006). F62, 980-983  [ doi:10.1107/S1744309106033884 ]

Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the biosynthetic N-acetylornithine aminotransferases from Salmonella typhimurium and Escherichia coli

V. Rajaram, K. Prasad, P. Ratna Prasuna, N. Ramachandra, S. R. Bharath, H. S. Savithri and M. R. N. Murthy

Synopsis: Acetylornithine aminotransferases, members of the type I subgroup II family of PLP-dependent enzymes, from S. typhimurium and E. coli have been cloned, overexpressed, purified and crystallized.

Online 19 September 2006


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Acta Cryst. (2006). F62, 984-985  [ doi:10.1107/S1744309106035640 ]

Preparation, crystallization and preliminary X-ray analysis of the methionine synthase (MetE) from Streptococcus mutans

T.-M. Fu, X.-Y. Zhang, L.-F. Li, Y.-H. Liang and X.-D. Su

Synopsis: Methionine synthase (MetE) from S. mutans was expressed, purified and crystallized. Diffraction data have been collected to 2.2 Å resolution.

Online 19 September 2006


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Acta Cryst. (2006). F62, 986-988  [ doi:10.1107/S1744309106034609 ]

Expression, purification, crystallization and preliminary X-ray analysis of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis

F. Moradian, C. Garen, L. Cherney, M. Cherney and M. N. G. James

Synopsis: Two enzymes responsible for arginine biosynthesis in M. tuberculosis were expressed in Escherichia coli, then purified to homogeneity. Preliminary X-ray analysis of diffraction-quality crystals grown from each enzyme are reported.

Online 30 September 2006


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Acta Cryst. (2006). F62, 989-992  [ doi:10.1107/S1744309106034464 ]

The purification, crystallization and preliminary structural characterization of FAD-dependent monooxygenase PhzS, a phenazine-modifying enzyme from Pseudomonas aeruginosa

N. Gohain, L. S. Thomashow, D. V. Mavrodi and W. Blankenfeldt

Synopsis: PhzS, an FAD-dependent monooxygenase that catalyzes a reaction involved in the biosynthesis of the virulence factor pyocyanin in P. aeruginosa, was cloned, overexpressed and crystallized. Data collection from native and seleno-L-methionine-labelled crystals is reported.

Online 30 September 2006


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Acta Cryst. (2006). F62, 993-995  [ doi:10.1107/S1744309106034476 ]

Crystallization and preliminary X-ray diffraction studies of a hyperthermophilic Rieske protein variant (SDX-triple) with an engineered rubredoxin-like mononuclear iron site

T. Iwasaki, A. Kounosu, D. Ohmori and T. Kumasaka

Synopsis: A hyperthermophilic archaeal Rieske iron-sulfur protein (sulredoxin) variant, SDX-triple (H44I/A45C/H64C), having a rationally designed rubredoxin-like mononuclear iron site in place of a Rieske [2Fe-2S] centre, has been crystallized. The P1 crystals of the SDX-triple variant diffract to 1.63 Å resolution using synchrotron radiation.

Online 30 September 2006


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Acta Cryst. (2006). F62, 996-998  [ doi:10.1107/S1744309106034701 ]

Crystallization and preliminary crystallographic study of carnosinase CN2 from mice

T. Yamashita, H. Unno, S. Ujita, H. Otani, N. Okumura, A. Hashida-Okumura, K. Nagai and M. Kusunoki

Synopsis: Mouse carnosinase was crystallized in complex with Zn2+ or Mn2+ and the complexes are undergoing structure determination by the MAD method.

Online 30 September 2006


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Acta Cryst. (2006). F62, 999-1002  [ doi:10.1107/S1744309106035433 ]

Cloning, crystallization and preliminary X-ray study of XC1258, a CN-hydrolase superfamily protein from Xanthomonas campestris

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

Synopsis: A CN-hydrolase superfamily protein from the plant pathogen X. campestris has been overexpressed in E. coli, purified and crystallized.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1003-1005  [ doi:10.1107/S1744309106035561 ]

Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae

J. Ohtsuka, K. Nagata, W. C. Lee, Y. Ono, R. Fukuda, A. Ohta and M. Tanokura

Synopsis: CTP:phosphoethanolamine cytidylyltransferase from S. cerevisiae has been expressed, purified and crystallized.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1006-1009  [ doi:10.1107/S1744309106035779 ]

Cloning, purification and preliminary crystallographic analysis of a putative pyridoxal kinase from Bacillus subtilis

J. A. Newman, S. K. Das, S. E. Sedelnikova and D. W. Rice

Synopsis: A putative pyridoxal kinase from B. subtilis has been cloned, overexpressed, purified and crystallized and data have been collected to 2.8 Å resolution.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1010-1012  [ doi:10.1107/S1744309106035901 ]

Expression, purification and crystallization of 2-oxo-hept-4-ene-1,7-dioate hydratase (HpcG) from Escherichia coli C

T. Adachi, A. Izumi, D. Rea, S.-Y. Park, J. R. H. Tame and D. I. Roper

Synopsis: The gene encoding HpcG from the homoprotocatechuate (4-hydroxyphenylacetic acid) degradative pathway of E. coli C has been cloned and expressed and the protein has been purified. Crystals obtained from the purified recombinant enzyme, belonging to a tetragonal space group, diffracted to a resolution of 2.1 Å.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1013-1015  [ doi:10.1107/S1744309106036074 ]

Crystallization and preliminary X-ray analysis of bacteriophage T4 UvsY recombination mediator protein

H. Xu, H. T. H. Beernink, M. A. Rould and S. W. Morrical

Synopsis: UvsY, the recombination mediator protein of bacteriophage T4, has been crystallized in both native and selenium-substituted forms. X-ray diffraction data have been collected to 2.2 Å.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1016-1017  [ doi:10.1107/S1744309106036098 ]

Crystallization and preliminary X-ray analysis of Atg3

Y. Yamada, N. N. Suzuki, Y. Fujioka, Y. Ichimura, Y. Ohsumi and F. Inagaki

Synopsis: S. cerevisiae Atg3, an E2-like enzyme that mediates the lipidation of Atg8, was crystallized and diffracted to 2.5 Å resolution.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1018-1020  [ doi:10.1107/S1744309106036256 ]

Crystallization and preliminary crystallographic analysis of p40phox, a regulatory subunit of NADPH oxidase

K. Honbou, S. Yuzawa, N. N. Suzuki, Y. Fujioka, H. Sumimoto and F. Inagaki

Synopsis: Human p40phox was expressed, purified and crystallized. Diffraction data were collected to a resolution of 3.0 Å.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1021-1023  [ doi:10.1107/S1744309106036232 ]

Expression, purification and crystallization of the Atg5-Atg16 complex essential for autophagy

M. Matsushita, N. N. Suzuki, Y. Fujioka, Y. Ohsumi and F. Inagaki

Synopsis: S. cerevisiae Atg5 in complex with the N-terminal regions of Atg16 was expressed, purified and crystallized in four crystal forms.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1024-1026  [ doi:10.1107/S174430910603661X ]

Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS

A. M. Balakrishna, Y.Y.-W. Tan, H.Y.-K. Mok, A. M. Saxena and K. Swaminathan

Synopsis: Crystals of the recombinant native and selenomethionine PilS protein belong to the orthorhombic space group P21212, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 Å. The structure will be solved using the MAD method.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1027-1030  [ doi:10.1107/S174430910603658X ]

Crystallization and preliminary crystallographic analysis of the transcriptional regulator RfaH from Escherichia coli and its complex with ops DNA

M. N. Vassylyeva, V. Svetlov, S. Klyuyev, Y. D. Devedjiev, I. Artsimovitch and D. G. Vassylyev

Synopsis: The E. coli transcriptional regulator RfaH was cloned, expressed, purified and crystallized and the complex of RfaH with its target DNA oligonucleotide was cocrystallized. Complete diffraction data sets were collected for the apo protein and its nucleic acid complex at 2.4 and at 1.6 Å resolution, respectively.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1031-1033  [ doi:10.1107/S1744309106036700 ]

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei

T. Yanagisawa, R. Ishii, R. Fukunaga, O. Nureki and S. Yokoyama

Synopsis: Pyrrolysyl-tRNA synthetase (PylRS) from M. mazei has been overexpressed in an N-terminally truncated form PylRS(c270) in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1034-1036  [ doi:10.1107/S1744309106036694 ]

Expression, purification and crystallization of L-methionine [gamma]-lyase 2 from Entamoeba histolytica

D. Sato, W. Yamagata, K. Kamei, T. Nozaki and S. Harada

Synopsis: L-Methionine [gamma]-lyase 2 from E. histolytica, a key enzyme in sulfur-containing amino-acid degradation in this protozoan parasite, has been crystallized in a form suitable for X-ray structure analysis.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1037-1040  [ doi:10.1107/S1744309106037535 ]

Crystallization and preliminary X-ray crystallographic studies of pig heart carbonyl reductase

K. Aoki, N. Tanaka, S. Ishikura, N. Araki, Y. Imamura, A. Hara and K. T. Nakamura

Synopsis: Pig heart carbonyl reductase has been crystallized in the presence of NADPH. Diffraction data have been collected using synchrotron radiation.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1041-1045  [ doi:10.1107/S1744309106038152 ]

A serendipitous discovery that in situ proteolysis is essential for the crystallization of yeast CPSF-100 (Ydh1p)

C. R. Mandel, D. Gebauer, H. Zhang and L. Tong

Synopsis: Proteolysis in situ by a protease secreted by a contaminating fungus is essential for the crystallization of yeast CPSF-100.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1046-1048  [ doi:10.1107/S1744309106038383 ]

The cloning, crystallization and preliminary X-ray analysis of XC2113, a YaeQ protein from Xanthomonas campestris

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

Synopsis: A YaeQ protein from the plant pathogen X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted well to a resolution of 1.28 Å.

Online 30 September 2006


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Acta Cryst. (2006). F62, 1049-1051  [ doi:10.1107/S1744309106038966 ]

Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase

A. T. Cordeiro, P. R. Feliciano and M. C. Nonato

Synopsis: Dihydroorotate dehydrogenase from L. major has been crystallized by the vapour-diffusion technique using lithium sulfate as the precipitant agent. A complete data set from a native crystal has been collected to 2.0 Å resolution using an in-house rotating-anode generator.

Online 30 September 2006


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