issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

June 2007 issue

Highlighted illustration

Cover illustration: Thermus thermophilus [Delta]1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+ [Inagaki, Ohshima, Sakamoto, Babayeva, Kato,Yokoyama & Tahirov (2007), Acta Cryst. F63, 462-465].

protein structure communications



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A crystal structure of NADP+-bound T. thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase refined to 1.55 Å resolution is reported. The structure provides structural insights into the mechanism of preference for coenzymes and enzyme activity.

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The crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) from Escherichia coli complexed with Mg2+, NADPH and fosmidomycin was determined at 2.2 Å resolution. The structure showed a well defined loop conformation at the active site of DXR.

crystallization communications


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Truncated rhodopsin from the retina of the squid Todarodes pacificus was extracted and crystallized by the sitting-drop vapour-diffusion method. Hexagonal crystals grown in the presence of octylglucoside and ammonium sulfate diffracted to 2.8 Å resolution.


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The cloning, expression, purification and crystallization of recombinant Clostridium perfringens β2-toxin is described. The crystals diffracted to 2.9 Å resolution.




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The NAD(P)H:ferredoxin oxidoreductase in carbazole 1,9a-dioxygenase from Janthinobacterium sp. J3 was crystallized and diffraction data were collected to 2.60 Å resolution.

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An α/β-type small, acid-soluble spore protein (SASP) from Bacillus subtilis, a major source of DNA protection against damaging effects in spores, was crystallized in a functionally relevant complex with a double-stranded DNA. This report provides insights into initial characterization of the complex and its structure elucidation.

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The M. tuberculosis protein Rv0765c was cloned, expressed, purified and crystallized. In an attempt to improve the quality of the crystals of Rv0765c, the protein was modified by reductive methylation. The methylated protein crystallized in a new crystal form with profoundly improved diffraction properties.

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A preliminary crystallographic study of cysteine synthase, a major enzyme in the cysteine-biosynthesis pathway, from the amoebic pathogen E. histolytica.

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Crystals of the oxidized form of the periplasmic nitrate reductase from Cupriavidus necator were obtained using polyethylene glycol 3350 as precipitant

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The electron-transfer complex of BphA3, a Rieske-type [2Fe–2S] ferredoxin, and BphA4, a NADH-dependent ferredoxin reductase, was crystallized by the sitting-drop vapour-diffusion method under anaerobic conditions.

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Cocrystallization with a peptide, free-interface diffusion crystal chips and crystal dehydration were important in the production of diffraction-quality crystals of the Munc18c protein that helps to regulate membrane fusion.

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The DIX domain of rat axin has been purified and crystallized. Crystals diffracted to 2.9 Å resolution using synchrotron radiation.

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PH1010, a DUF54-family protein from the hyperthermophilic archaeon P. horikoshii OT3, was crystallized and X-ray diffraction data were collected to 1.90 Å resolution.

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Recombinant TnC was expressed in Escherichia coli, purified, complexed with a 24-residue synthetic peptide derived from scallop troponin I (TnI) and crystallized.

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The [NiFe] hydrogenase maturation proteins HypC and HypD were purified and crystallized. Crystals of HypC and HypD suitable for data collection diffracted to 1.80 and 2.07 Å resolution, respectively.

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Crystallization and preliminary diffraction data of the N-terminal 19–139 fragment of the origin-binding domain of bacteriophage λ O replication initiator are reported.
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