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The crystal structure of S. aureus cytidine monophosphate kinase in complex with cytidine 5′-monophosphate has been determined.
Two new crystal structures of A. niger α-amylase are reported, one of which reveals two hitherto unobserved maltose-binding sites.
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.
The crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942 was determined at 2.9 Å resolution.
RuvA, a protein from M. tuberculosis H37Rv involved in recombination, has been cloned, expressed, purified and analysed by X-ray crystallography.
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.
The crystallization of rice α-amylase/subtilisin bifunctional inhibitor is reported.
This is the first report of the crystallization of an IDS-epimerase from A. tumefaciens BY6 and its l-selenomethionine derivative.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
The expression, purification and preliminary X-ray diffraction analysis of a catalytic domain of a chitinase from P. furiosus is reported.
M. tuberculosis N-succinyldiaminopimelate aminotransferase, the enzyme which catalyzes the sixth reaction in the lysine-biosynthesis pathway, has been cloned, expressed, purified and crystallized.
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.
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.
A glyoxalase II from L. infantum was cloned, purified and crystallized and its structure was solved by X-ray crystallography.
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.
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.
The phasin PhaPAh from A. hydrophila strain 4AK4 was crystallized using the hanging-drop vapour-diffusion method.
Cross crystallization is reported as a new crystallization procedure used for growing protein crystals and preliminary diffraction analysis of a newly discovered protein, cytochrome c 4, is reported.
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).