issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2009 issue

Highlighted illustration

Cover illustration: The ligand-binding domain of the EphB2 receptor (Goldgur et al., p. 71).

protein structure communications


Acta Cryst. (2009). F65, 67-70
doi: 10.1107/S1744309108037342
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The X-ray crystal structure of the Trx-fold domain of hPDCL2 was solved at 2.70 Å resolution and resembled the Trx-fold domain of rat phosducin.

Acta Cryst. (2009). F65, 71-74
doi: 10.1107/S1744309108043078
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The crystal structure of the ligand-binding domain of a receptor tyrosine kinase EphB2, an important mediator of cell-cell communication, has been determined at a resolution of 2 Å. The structure confirms the induced-fit mechanism for the binding of ligands to EphB receptors.

Acta Cryst. (2009). F65, 75-79
doi: 10.1107/S1744309108043194
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The crystal structure of human protein kinase CK2α2 with a potent indazole-derivative inhibitor has been determined at 3.2 Å resolution.

Acta Cryst. (2009). F65, 80-83
doi: 10.1107/S1744309108044114
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X-ray structures of ferric cytochrome P450cam partially complexed with the substrate (+)-camphor to two different extents were determined at 1.30–1.35 Å resolution, revealing the protein structures of the substrate-free and substrate-bound forms.

Acta Cryst. (2009). F65, 84-92
doi: 10.1107/S1744309109001110
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The crystal structure of iron superoxide dismutase from the cold-adapted organism A. salmonicida has been determined at a resolution of 1.7 Å.

crystallization communications


Acta Cryst. (2009). F65, 93-97
doi: 10.1107/S1744309108042425
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The crystallization and X-ray analysis of recombinant human cytosolic phenylalanyl-tRNA synthetase (hcPheRS) are reported. Diffraction data were collected to 3.3 Å resolution and the hcPheRS structure was determined by the molecular-replacement method using phase information derived from multiwavelength anomalous dispersion data.

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Various E. coli tRNAArg acceptor-stem microhelix isoacceptors have been crystallized and investigated by high-resolution X-ray diffraction analysis.

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The human cytokine IL-22 has been crystallized in complex with its soluble decoy receptor IL-22BP. Diffraction data were collected to 2.75 Å resolution; the crystals belonged to the tetragonal space group P41.

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The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 K using the hanging-drop vapour-diffusion method.

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The second RRM of Pub1 from S. cerevisiae was overexpressed, purified and crystallized. Diffraction data were collected to 1.69 Å resolution.

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Degradation-free crystalization of thrombin-digested recombinant His-tagged PsbP protein of photosystem II from Spinacia oleracea resulting in crystals diffracting to 2.06 Å.

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The hexameric Cu-containing nitrite reductase and its electron-donor protein pseudoazurin have been cocrystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 3.3 Å resolution using a synchrotron-radiation source.

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Crystallization of pigeon haemoglobin at low pH (5.5) and high ionic concentration (1 M) using the hanging-drop vapour-diffusion method is reported.

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The soluble domain of a putative copper-containing nitrite reductase from P. acnes has been overexpressed, purified and crystallized. The crystal belonged to space group P213 and diffracted to 2.4 Å resolution.

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Preliminary X-ray analysis of crystals of the bacterial microcompartment shell protein Eut-L from Escherichia coli is reported.

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The catalytic module of a family 101 glycoside hydrolase from S. pneumoniae was cloned, recombinantly produced and crystallized.

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Two C-terminally truncated variants of the small subunit of isopropylmalate isomerase from M. tuberculosis have been cloned, expressed, purified, crystallized and examined by X-ray diffraction.

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Crystallization of CcCel6C was carried out by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.6 Å resolution from the crystal.

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The C-terminal domain protein of the PB2 subunit of influenza A virus RNA-dependent RNA polymerase was expressed and crystallized and diffraction data were obtained from the crystals.

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Crystals of the 45.1 kDa functional form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from B. subtilis diffracted to 2.30 Å resolution.

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A complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. Crystals of this intramolecular complex diffracted to 2.16 Å resolution.

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The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the transcriptional repressor SirR (staphylococcal iron regulator) from M. tuberculosis are reported.

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The chromophore-binding domain of cyanobacteriochrome AnPixJ was overproduced in E. coli, purified and crystallized in its red-absorbing form. Diffraction data were then collected to a resolution of 1.8 Å.

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Native and selenomethionine-labeled crystals of Ebola VP35 interferon inhibitory domain were obtained by the hanging-drop vapor-diffusion method.

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An alkaline alanine racemase from alkaliphilic B. pseudofirmus OF4 was expressed in E. coli and purified. Crystallization and preliminarily X-­ray crystallographic analysis were performed for the recombinant enzyme.

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The yeast N-acetyltransferase that N-acetylates L-azetidine-2-carboxylic acid has been crystallized. Native data were collected to 1.9 Å resolution from a substrate-soaked crystal.

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Rv1653, an ornithine acetyltransferase from M. tuberculosis, has been crystallized and diffraction data have been collected to 1.7 Å resolution.

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Crystals of adeno-associated virus serotype 3b, a human DNA virus with promise as a vector for gene therapy, have been grown, diffract X-rays to ∼2.6 Å resolution and are suitable for structure determination in spite of twinning.

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Preliminary neutron crystallographic data from the serine protease proteinase K have been recorded using the LADI-III diffractometer at the Institut Laue–Langevin. The results illustrate the feasibility of a full neutron structural analysis aimed at further understanding the catalytic mechanism of proteinase K.

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Dihydrodipicolinate synthase (DHDPS) catalyses an important step in lysine biosynthesis. Here, the expression, purification, crystallization and preliminary diffraction analysis to 2.15 Å resolution of DHDPS from B. anthracis soaked with the substrate pyruvate are reported.
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