issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

May 2012 issue

Highlighted illustration

Cover illustration: Hansenula polymorpha copper amine oxidase-1 in complex with CoII (Klema et al., p. 501).

structural communications


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The structure of copper amine oxidase 1 from H. polymorpha in its metal-free precursor (apo) form is reported along with structures of the apo protein in complex with CuI and CoII.

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Hexameric rings of RadA recombinase from M. voltae have been crystallized. Structural comparisons suggest that homologues of RadA tend to form double-ringed assemblies.

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A new crystal structure of yeast Rpn14 with an E384A mutation was determined at 1.6 Å resolution. The improved high-resolution structure provides a framework for understanding proteasome assembly.

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The crystal structure of the C61S mutant of Tpx from E. coli is reported at 1.97 Å resolution. A brief structural comparison with homologues is presented.

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The structure of the catalytic chain of Methanococcus jannaschii aspartate transcarbamoylase has been determined in a hexagonal crystal form and gives insight into the possible paths that the substrate carbamoyl phosphate may follow to reach the active site during catalysis.

crystallization communications



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Carbonyl reductase S1 from C. magnoliae was expressed, purified and crystallized. The crystals obtained diffracted X-rays to 1.90 Å resolution and belonged to space group P6122 or P6522.

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A cell membrane permeable SOD, SOD-TAT fusion protein, was expressed, purified and crystallized. X-ray diffraction data have been collected to 3.2 Å resolution.

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A novel hyperactive antifreeze protein from R. inquisitor (RiAFP) has been overexpressed, purified and crystallized. A complete native X-ray diffraction data set was recorded to 1.3 Å resolution.

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3-Ketosteroid Δ1-dehydrogenase from Rhodococcus erythropolis SQ1 was successfully crystallized and its initial structure was solved.


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Esterase A from C. crescentus CB15 was crystallized in space group C2221 and diffraction data were collected to a resolution of 1.62 Å.

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Two hypothetical ribose-5-phosphate isomerases from S. mutans have been produced in E. coli and crystallized. The crystals diffracted to high resolutions suitable for crystallographic analyses.

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The Crimean–Congo haemorrhagic fever virus nucleocapsid protein was expressed in E. coli, purified and crystallized. X-ray diffraction data were collected to 2.1 Å resolution.

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A trypsin-resistant catalytic domain of human calcineurin α (A subunit, residues 20–347) was crystallized in space group P21212. An X-ray diffraction data set was collected to 2.87 Å resolution and the structure was solved by molecular replacement.

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The major capsid proteins VP16 and VP17 of bacteriophage P23-77 have been crystallized using both recombinant and purified virus and preliminary diffraction analyses have been performed.

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The expression, purification and crystallization of the alginate lyase AlgL from P. aeruginosa is described. The crystals diffracted to a resolution of 1.64 Å.

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Crystals of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3 belonged to space group P21 and contained two heterotetramers in the asymmetric unit related by 222 noncrystallographic symmetry. X-ray data were collected to a maximum resolution of 2.5 Å using a synchrotron source.

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The crystallization and preliminary X-ray diffraction analysis of a novel chloromuconolactone dehalogenase from R. opacus 1CP are described. The oligomeric state was determined based on the self-rotation function.

laboratory communications


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The utility of differential scanning fluorimetry for homogeneity assessment and crystallization improvement of PLP-dependent enzymes is demonstrated using the potential drug target BioA from M. tuberculosis.

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An on-column ligand- and detergent-exchange method was developed to obtain ligand–protein complexes for an adamantane series of compounds with 11β-HSD1 after a variety of other complexation methods had failed. An interesting byproduct of the method was the observation of artificial trimers in the crystal structures.

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Addition of protease instead of seeds using a robot can be used to optimize the concentration of protease in in situ proteolysis experiments and has been successfully tested using two proteins.
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