issue contents

ISSN: 2053-230X

January 2007 issue

Highlighted illustration

Cover illustration: Crystals from articles published in Acta Cryst. Section F during 2006. Top row (left to right): LTP2-like resistance signalling protein DIR1 (Lascombe et al., pp. 702-704); YaeQ protein XC2113 (Chio et al., pp. 1046-1048); arginine-biosynthetic enzyme from M. tuberculosis (Moradian et al., pp. 986-988). Bottom row (left to right): native PRONE8 and its SeMet derivative (Thomas et al., pp. 607-610); bacteriophage T4 UvsY recombination mediator protein (Xu et al., pp. 1013-1015); 6-­aminohexanoate-cyclic-dimer hydrolase (Yasuhira et al., pp. 1209-1211).

protein structure communications

Acta Cryst. (2007). F63, 1-6
doi: 10.1107/S1744309106046823
link to html
The crystal structure of MtSK in complex with ADP shows conformational changes caused by the absence of the shikimate molecule, and the effect of chloride ions on the nucleotide binding site, and the crystal structure of MtSK in absence of magnesium shows its effect on the shikimate binding site.

Acta Cryst. (2007). F63, 7-11
doi: 10.1107/S1744309106051773

crystallization communications

Acta Cryst. (2007). F63, 12-14
doi: 10.1107/S1744309106051530
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The DNA methyltransferase M.BseCI from B. stearothermophilus was crystallized as a complex with its cognate DNA. Crystals belong to space group P6 and diffract to 2.5 Å resolution at a synchrotron source.

Acta Cryst. (2007). F63, 15-17
doi: 10.1107/S1744309106051578
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An archaeal 6-pyruvoyl tetrahydrobiopterin synthase homologue from P. horikoshii OT3 was overexpressed as native and selenomethionine-substituted protein, purified and crystallized. The native and selenomethionine-derivative crystals are isomorphous and diffract X-rays to 2.1 and 2.9 Å resolution, respectively.

Acta Cryst. (2007). F63, 18-20
doi: 10.1107/S1744309106051682

Acta Cryst. (2007). F63, 21-23
doi: 10.1107/S1744309106051955
link to html
The caspase-recruitment domain of the cytosolic pathogen receptor Nod1 was crystallized. X-ray diffraction data were collected to 1.9 Å resolution.

Acta Cryst. (2007). F63, 24-26
doi: 10.1107/S1744309106052341
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The avian infectious bronchitis virus main protease has been crystallized; crystals diffract to 2.7 Å resolution.

Acta Cryst. (2007). F63, 27-29
doi: 10.1107/S1744309106052560
link to html
The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P21 and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively.

Acta Cryst. (2007). F63, 30-33
doi: 10.1107/S1744309106052730
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A conserved hypothetical protein Se-XC5848 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. Crystals obtained from the purified recombinant protein diffracted to a resolution of 1.68 Å.

Acta Cryst. (2007). F63, 34-36
doi: 10.1107/S1744309106053127
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The transcriptional regulator CmeR from C. jejuni has been purified and crystallized and X-ray diffraction data have been collected to a resolution of 2.2 Å.

Acta Cryst. (2007). F63, 37-41
doi: 10.1107/S174430910604509X
link to html
The crystallization and structure determination of the apo form of a novel haem-containing Tat substrate, YcdB from E. coli, has been solved to 2.0 Å resolution. The preliminary structure shows similarity to other haem-dependent peroxidases, despite low sequence homology.

Acta Cryst. (2007). F63, 42-45
doi: 10.1107/S1744309106052924
link to html
Diisopropyl fluorophosphatase (DFPase) effectively hydrolyzes a number of organophosphorus nerve agents, including sarin, cyclohexylsarin, soman and tabun. Neutron diffraction data have been collected from DFPase crystals to 2.2 Å resolution in an effort to gain further insight into the mechanism of this enzyme.

Acta Cryst. (2007). F63, 46-48
doi: 10.1107/S1744309106052870
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In order to investigate the identity elements of the E. coli tRNAGly/GlyRS class II system, a tRNAGly acceptor-stem microhelix was crystallized and a data set was collected to 2.0 Å resolution using synchrotron radiation.

Acta Cryst. (2007). F63, 49-51
doi: 10.1107/S1744309106054145
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The radixin FERM domain has been crystallized in complex with CD43 and PSGL-1 peptides. Diffraction data sets were collected from the complexes to 2.9 and 2.8 Å resolution, respectively.

Acta Cryst. (2007). F63, 52-55
doi: 10.1107/S1744309106054522

Acta Cryst. (2007). F63, 56-58
doi: 10.1107/S1744309106054509
link to html
The putative thiamine-biosynthesis protein PH1313 from P. horikoshii OT3 was overexpressed, purified and crystallized. The crystals belong to space group P212121 and diffract X-rays to 1.9 Å resolution.

addenda and errata

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