issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

August 2006 issue

Highlighted illustration

Cover illustration: Rv2074, a probable pyridoxine 5'-phosphate oxidase from Mycobacterium tuberculosis, at 1.6 Å resolution (p. 735).

protein structure communications


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The crystal structure of S. aureus cytidine monophosphate kinase in complex with cytidine 5′-monophosphate has been determined.

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Two new crystal structures of A. niger α-amylase are reported, one of which reveals two hitherto unobserved maltose-binding sites.

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Two structures of the enzyme phosphomannomutase/phosphoglucomutase in complex with ribose 1-phosphate and xylose 1-phosphate are described. Despite structural differences from the enzyme's preferred phosphohexose substrates, both ligands trigger the interdomain rotation required for catalysis.

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The crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942 was determined at 2.9 Å resolution.

structural genomics communications


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RuvA, a protein from M. tuberculosis H37Rv involved in recombination, has been cloned, expressed, purified and analysed by X-ray crystallography.

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The crystal structure of a probable pyridoxine 5′-phosphate oxidase, Rv2074 from M. tuberculosis, has been solved by the two-wavelength anomalous dispersion method and has been refined at 1.6 Å resolution. Two citric acid molecules are bound fortuitously to the possible active site of Rv2074.

crystallization communications



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This is the first report of the crystallization of an IDS-epimerase from A. tumefaciens BY6 and its L-selenomethionine derivative.

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The digestive lysozymes 1 and 2 from M. domestica were crystallized by vapour diffusion. The crystallographic data were processed to a maximum resolution of 1.9 Å in both cases.

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M. tuberculosis hypothetical protein Rv2827c was cloned, expressed, purified and crystallized. Preliminary X-ray diffraction data were collected to a resolution of 1.93 Å.

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Recombinant D. radiodurans TrxR with a His tag at the N-terminus was expressed in Escherichia coli and purified by metal-affinity chromatography. The protein was crystallized using the sitting-drop vapour-diffusion method in the presence of 35% PEG 4000, 0.2 M ammonium acetate and citric acid buffer pH 5.1 at 293 K.

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BipD is likely to be a component of a type-III protein secretion system (TTSS) in B. pseudomallei. Native and selenomethionyl-BipD proteins have been expressed and crystals have been obtained which diffract to 2.1 Å.

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A myotoxic Asp49-PLA2 with low catalytic activity from B. jararacussu (BthTX-II) was crystallized in the monoclinic crystal system; a complete X-ray diffraction data set was collected and a molecular-replacement solution was obtained. The oligomeric structure of BthTX-II resembles those of the Asp49-PLA2 PrTX-III and all bothropic Lys49-PLA2s.

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Two methyltransferases from flaviviruses (Meaban and Yokose viruses) have been overexpressed and crystallized. Diffraction data and characterization of the two crystal forms are presented, together with a preliminary molecular-replacement solution for both enzymes.

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Prophenoloxidase (proPO) activating factor-I (PPAF-I) is a catalytically active clip-domain SP, cleaves which proPO. The results of crystallization and preliminary X-ray analysis of the SP domain of PPAF-I are reported here.

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The catalytic domain of the murine glycosyltransferase Manic Fringe was expressed in insect cells. Removal by site-directed mutagenesis of two N-glycosylation sites present in the protein was essential to obtain crystals that diffracted to 1.8 Å resolution.

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SA0961 is an unknown hypothetical protein from Staphylococcus aureus that can be identified in the Firmicutes division of Gram-positive bacteria. SA0961 was cloned and the protein was overexpressed in Escherichia coli, purified and subsequently crystallized.

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Type 1 RNase H from the hyperthermophilic archaeon S. tokodaii 7 was overproduced in E. coli, purified, and crystallized. Preliminary crystallographic studies indicated that the crystal belongs to space group P43, with unit-cell parameters a = b = 39.21, c = 91.15 Å.

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Transportin 1 was cocrystallized with nucleocytoplasmic shuttling fragments of JKTBP and hnRNP D and a nuclear localization fragment of TAP. X-ray diffraction data were collected using synchrotron radiation at SPring-8.

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The archaeal phosphoglycerate mutase PH0037 from P. horikoshii OT3 has been crystallized in space group R32, with unit-cell parameters a = 155.62, c = 230.35 Å. A 2.2 Å resolution data was collected at SPring-8 beamline BL26B1.

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The expression, purification and preliminary X-ray diffraction analysis of a catalytic domain of a chitinase from P. furiosus is reported.

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M. tuberculosis N-succinyldiaminopimelate aminotransferase, the enzyme which catalyzes the sixth reaction in the lysine-biosynthesis pathway, has been cloned, expressed, purified and crystallized.

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Rice BGlu1 β-glucosidase was purified from recombinant E. coli and crystallized with and without the inhibitor 2-deoxy-2-fluoro-β-D-glucose. The crystals diffracted to 2.15 and 2.75 Å, respectively.

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The nonstructural protein VP9 from white spot syndrome virus (WSSV) has been identified and expressed in Escherichia coli. Native protein was purified and crystallized by vapour diffusion.


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Recombinant oligopeptidase B from T. brucei has been prepared and crystallized. Data were collected to 2.7 Å. Heavy-atom soaks and preparation of selenomethionine-substituted protein are in progress for structure determination by MAD or MIR.

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Mouse myo-inositol oxygenase, a key enzyme involved in inositol catabolism, has been expressed, purified and crystallized in a form suitable for structure determination by X-ray crystallography.

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The phasin PhaPAh from A. hydrophila strain 4AK4 was crystallized using the hanging-drop vapour-diffusion method.

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Cross crystallization is reported as a new crystallization procedure used for growing protein crystals and preliminary diffraction analysis of a newly discovered protein, cytochrome c4, is reported.

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This paper describes the crystallization, dehydration and preliminary X-ray data analysis of a complex containing several bacteriophage lambda excisionase (Xis) proteins cooperatively bound to a 33-mer DNA duplex (Xis–DNAX1-X2).
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