issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

June 2008 issue

Highlighted illustration

Cover illustration: Rat fibroblast growth factor 1 crystallized in the presence of sucrose octasulfate (Kulahin et al., p. 448).

protein structure communications


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In this paper, the 1.2 Å atomic resolution crystal structure of the 5-nitroimidazole antibiotic resistance protein NimA from Deinococcus radiodurans (DrNimA) is presented.

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The work describes the sucrose octasulfate-mediated dimerization of rat FGF1 by gel-filtration experiments and crystal structure determination.

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The crystal structure of an N-terminally (25 residues) truncated fragment of selenophosphate synthetase (SPS-ΔN) from Aquifex aeolicus has been determined at 2.0 Å resolution.

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The three-dimensional structure of a SARS coronavirus-derived peptide, VQQESSFVM, bound to the human major histocompatibility complex (MHC) class I antigen HLA-B*1501 is presented.

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Partial dehydration of high-salt horse methaemoglobin crystals tends to shift the structure from the R state to the R2 state, in agreement with previous observations that movements in the molecule resulting from changes in water content mimic those involved in protein action.

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The crystal structure of the core-binding domain of bacteriophage lambda integrase has been determined at 2.0 Å resolution.

structural genomics communications


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T. brucei gene Tb10.6k15.0140 codes for an α/β-hydrolase fold protein of unknown function. The 2.2 Å crystal structure shows that members of this sequence family retain a conserved Ser residue at the expected site of a catalytic nucleophile, but that trypanosomatid sequences lack structural homologs for the other expected residues of the catalytic triad.

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The 1.95 Å resolution X-ray crystal structure of tunicamycin-resistance protein (TmrD) from D. radiodurans is described.

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Three conventional robots were subjected to a crystallization screening test involving 18 proteins from T. thermophilus HB8 using the sitting- and hanging-drop vapour-diffusion and microbatch methods. The number of diffraction-quality crystals and the amount of time required to obtain visible crystals depended greatly on the robots used. The combined use of different robots, especially for protein samples exhibiting low crystallization success rates, significantly increased the chance of obtaining diffraction-quality crystals.

crystallization communications


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CMS1MS2, a cysteine proteinase from C. candamarcensis, displays high amidase activity against the substrate BAPNA. The enzyme was purified and crystallized by the hanging-drop method and preliminary diffraction data were collected to 1.8 Å resolution.

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Mcm10 is a highly conserved nuclear protein that plays a key role in the initiation and elongation processes of DNA replication by providing a physical link between the Mcm2–7 complex and DNA polymerases. In this study, the central domain of human Mcm10 was crystallized using the hanging-drop vapour-diffusion method in the presence of PEG 3350.

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The putative ABC transporter ATP-binding protein TM0222 from T. maritima was cloned, overproduced, purified and crystallized. A complete MAD diffraction data set has been collected to 2.3 Å resolution.

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Crystallization of the prefoldin β subunit Yke2 is reported. This protein is a novel and potentially important target for anti-cancer therapeutics.

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Recombinant G. cingulata cutinase has been overexpressed and the protein has been purified and crystallized in the absence or presence of inhibitors.

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NCDV VP8*64–224 was expressed in E. coli, purified and crystallized in the presence of a sialic acid derivative. X-ray diffraction data were obtained to a resolution of 2.0 Å and the crystallographic structure was determined by molecular replacement.

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CapF, a capsular polysaccharide-assembling protein from S. aureus, has been crystallized using the hanging-drop vapour-diffusion method. Oprimization of the crystallization conditions by differential scanning calorimetry afforded a crystal of selenomethionine-substituted CapF that diffracted to a resolution of 2.80 Å.

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Recombinant human chondroadherin has been crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to the monoclinic space group P21 and diffracted to at least 2.3 Å resolution.

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The biotin protein ligase from S. aureus has been overexpressed in E. coli, purified, crystallized by the hanging-drop vapour-diffusion method and analysed using X-ray diffraction.

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The cloning, purification, crystallization and preliminary X-ray characterization of the crystals of biotin acetyl-CoA carboxylase ligase from M. tuberculosis are reported.


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Human prouroguanylin, a precursor protein of a peptide hormone, was expressed in E. coli, refolded, purified and crystallized. The crystals belong to space group P6122 and diffract X-rays to 2.5 Å resolution.

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The predicted eight-stranded β-barrel outer membrane protein TTC0834 from T. thermophilus HB27 was overexpressed in T. thermophilus HB8 and crystallized. Diffraction data were collected to a maximal resolution of 3.2 Å.

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The crystallization and preliminary neutron crystallographic analysis of selectively CH3-protonated deuterated rubredoxin from P. furiosus is presented. This work represents the first reported use of selectively labeled material for phasing applications using neutron protein crystallography.

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MtbCysA3, a probable rhodanese-like thiosulfate sulfurtransferase, has been expressed, purified and crystallized. Preliminary X-ray analysis shows a dimer in the asymmetric unit.

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Sagitoxin, a novel cardiotoxin from the venom of Naja naja saggitifera, has been successfully isolated, purified to homogeneity and crystallized.

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The production and purification of recombinant SoGST3 and SoGST6, two GST-like proteins from S. oneidensis, are reported and preliminary crystallographic studies of crystals of the recombinant enzymes are presented.

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PhnP, a member of the C—P lyase pathway, was crystallized by the sitting-drop vapour-diffusion method and the initial diffraction-pattern analysis is reported.

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The crystallization of VinC, a glycosyltransferase involved in the biosynthesis of the antitumour antibiotic vicenistatin, is reported.

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The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of H. pylori MotB, a peptidoglycan-binding component of the stator of the bacterial flagellar motor, are reported.

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X-ray diffraction data from the targeting (FAT) domain of focal adhesion kinase (FAK) were collected from a single crystal that diffracted to 1.99 Å resolution.

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This work describes the optimization of hemimethylated DNA duplexes for co-crystallization with a dimeric SeqA mutant, as well as the preliminary characterization of the SeqA–DNA co-crystals.
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