issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

May 2009 issue

Highlighted illustration

Cover illustration: Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate (Cameron et al., p. 450).

structural communications


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The structure of pig heart citrate synthase was solved at 1.78 Å resolution. Cys184 was inadvertently modified through disulfide exchange with a component of the crystallization mixture.

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The structure of M. tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) was determined by the molecular-replacement method to 3.4 Å resolution in space group I432 and was refined to a final Rwork and Rfree of 0.285 and 0.321, respectively.

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Crystal structures of the ubiquitin-conjugating enzyme E2-25K M172A mutant protein at pH 6.5 and pH 8.5 were determined to 1.9 and 2.2 Å resolution, respectively. Examination of the structures revealed domain–domain interactions between the UBC and UBA domains which have not previously been reported.

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The Nac1 POZ domain resembles the POZ-domain dimers of the POZ-zinc finger transcription factors; the structure will have relevance for the design of therapeutics that target Nac1 function in ovarian cancer.

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The structure of 6-phosphogluconate dehydrogenase from a moderate thermophile, G. stearothermophilus, is presented and compared with those of orthologous enzymes.

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The crystal structures of TTHA1623 from T. thermophilus HB8 in an iron-bound and a zinc-bound form have been determined to 2.8 and 2.2 Å resolution, respectively.

crystallization communications


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The ketoacyl-acyl carrier protein synthase III (KASIII) encoded by the fabH gene of X. oryzae pv. oryzae is responsible for elongation by two C atoms in fatty-acid synthesis. The fabH gene was cloned, the KASIII enzyme was expressed and preliminary crystallographic study was performed with the aim of understanding the reaction mechanism.

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The expression, purification, refolding and crystallization of the outer membrane protein AlgE from P. aeruginosa is described. The crystals diffracted to 3.0 Å resolution.

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The recombinant form of the allergen Can f 2 from C. familiaris was produced, isolated and crystallized in two different forms. Preliminary X-ray diffraction analyses are reported for the two crystal forms of Can f 2.

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The TON_0887 gene product was purified and crystallized at 295 K. A 2.2 Å resolution data set was collected using synchrotron radiation.

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Glutathione S-transferases (GSTs) are a group of detoxifying enzymes that are found in animals, plants and microorganisms. Here, the crystallizations of two cyanobacterial GSTs are reported with the aim of determining their atomic structures.

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The crystallization of the receiver domain of the histidine kinase CYTOKININ-INDEPENDENT1 from A. thaliana is described. The crystals diffracted to 2.0 Å resolution.

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The crystallization and results of multiwavelength anomalous diffraction studies of a recombinant C3-inhibitory fragment of Efb from S. aureus are reported.

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The bifunctional enzyme catalase-phenol oxidase from S. thermophilum was crystallized by the hanging-drop vapour-diffusion method in space group P21 and diffraction data were collected to 2.8 Å resolution.

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Get3 is a cytosolic ATPase which can recognize and bind the transmembrane domain of tail-anchored proteins. Yeast Get3 has been crystallized and the crystals diffracted to 2.7 Å resolution using a synchrotron X-ray source.

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Laminin-binding protein from S. agalactiae was expressed, purified and crystallized and X-ray diffraction data were collected to 2.5 Å resolution.

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A joint X-ray and neutron crystallographic study has been initiated to determine the specific water network and the protonation states of the hydrophilic residues that coordinate it in human carbonic anhydrase II.

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XynC, a glycosyl hydrolase family 5 xylanase from B. subtilis, has been purified and crystallized with the primary goal of structural determination and characterization of a second xylanase from this large catalytically diverse glycosyl hydrolase family.

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Mouse endonuclease G without its mitochondrial localization signal (amino-acid residues 1–43) was successfully overexpressed, purified and crystallized using a microbatch method under oil.

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A. aeolicus GidA has been crystallized in two different crystal forms: forms I and II. X-ray diffraction data were collected to 3.2 and 2.3 Å resolution, respectively, using a synchrotron-radiation source.

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A protease-resistant mutant form of human galectin-8 has been crystallized and diffraction data have been collected to 3.4 Å resolution.

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The crystallization of an alginate-binding protein isolated from Sphingomonas sp. A1 and the results of preliminary crystallographic analysis of this protein are presented.

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The preliminary X-ray data of β-microseminoprotein isolated from human seminal plasma at 2.4 Å resolution are reported.

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The first crystallographic study of a plant subtilase, SBT3 from S. lycopersicum, is reported.

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The gene that encodes human coronavirus HKU1 nonstructural protein 9 was cloned and expressed in Escherichia coli and the protein was subjected to crystallization trials.

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Human ADP-ribosylhydrolase 1, which cleaves the glycosidic bond between ADP-ribose and specific Arg residues in proteins, has been cloned, expressed, purified and crystallized.

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A recombinant serine protease inhibitor, CrSPI-1, from horseshoe crab, which inhibits subtilisin with a Ki of 10−9M, has been cloned, expressed, purified and cocrystallized with subtilisin. The crystals diffracted to 2.6 Å resolution.

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Isocitrate dehydrogenase kinase/phosphatase has been crystallized in three different crystal forms. Data were collected from each crystal form for structure determination.
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