issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

May 2010 issue

Highlighted illustration

Cover illustration: mAG, a monomeric mutant of the green fluorescent protein Azami-Green (Ebisawa et al., p. 485).

structural communications



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The first crystal structure of phosphoglucose isomerase from M. tuberculosis H37Rv is reported.

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The crystal structure of OPRTase from the caries pathogen Streptococcus mutans is reported at 2.4 Å resolution.

crystallization communications


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In order to determine the structure–function relationship of the azo-dye reduction mechanism, an X-ray crystallographic study of azoreductases was performed. Selenomethionine-labelled AzrA (SeMet-AzrA) and AzrC were crystallized by the hanging-drop vapour-diffusion method.

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The purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from MRSA252 in the apo form is reported.

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A female-specific lacrimal protein from Syrian hamsters has been crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffraction data were collected to 1.86 Å resolution.

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Crystals of C-terminally His-tagged ThyX from H. pylori belonged to space group C2, with unit-cell parameters a = 221.92, b = 49.43, c = 143.02 Å, β = 98.84°, and diffracted to beyond 2.5 Å resolution.

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N-terminal fragments of the cyclic AMP receptor protein from E. coli created by two different proteases, subtilisin and chymotrypsin, have been crystallized and diffracted to 2.0 and 2.8 Å resolution, respectively.

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The endonuclease/exonuclease/phosphatase-homology domain of phosphodiesterase PDE12 has been crystallized. The crystals diffracted to 2.5 Å resolution.

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Selenomethionine-derivatized glutamate dehydrogenase from P. asaccharolyticus has been crystallized. Diffraction data were collected to 3.5 Å resolution from crystals belonging to the rhombohedral space group H32 and structure determination is in progress.

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H. pylori MinE has been expressed, purified and crystallized. Native and MAD data sets have been collected from H. pylori MinE crystals to 2.8 and 3.0 Å resolution, respectively.

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The SMU.2055 gene from the major caries pathogen Streptococcus mutans was cloned and native and SeMet-labelled SMU.2055 proteins were expressed at a high level. Diffraction-quality crystals of SeMet-labelled SMU.2055 were obtained using the sitting-drop vapour-diffusion method and diffracted to a resolution of 2.5 Å.

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Two soluble His-tagged forms of the lytic transglycosylase MltF, one containing full length protein, the other containing its N-terminal domain, have been successfully overexpressed, purified and crystallized. X-ray diffraction data were collected for both crystal forms, including a MAD data set to 2.7 Å for the MltF N-terminal domain.

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Triclinic crystals of a self-complementary DNA heptacosamer with 20-base-pair duplexes flanked by 3′-terminal seven-nucleotide overhangs have been obtained. X-ray data were collected to 2.8 Å resolution using synchrotron radiation.

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The N-terminal carbohydrate-recognition domain of human galectin-4 has been crystallized by the vapour-diffusion technique using polyethylene glycol as the precipitant agent. A complete data set was collected from a native crystal to 2.2 Å resolution.

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A soluble domain spanning amino-acid residues 16–197 of the Drosophila Dribble protein was overexpressed in E. coli, purified and crystallized. X-ray diffraction data were collected to beyond 2 Å resolution.

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The Fe2+-dependent dioxygenase NicX from P. putida KT2440 has been crystallized using the vapour-diffusion method. Native data have been collected to 2.0 Å resolution.

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The macrophage growth locus A (MglA) protein from F. tularensis crystallized in the hexagonal space group P61 or P65, with unit-cell parameters a = b = 125, c = 54 Å.

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Crystals of infectious West Nile virus were obtained and diffracted at best to about 25 Å resolution. Preliminary analysis of the diffraction pattern suggested tight hexagonal packing of the intact virus.

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The RNA-binding protein Hfq from B. subtilis was crystallized using the hanging-drop vapour-diffusion method in two crystal forms that belonged to space groups I422 and F222; diffraction data were collected to 2.2 Å resolution from both forms.

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The N-terminal domain of ING4 was overexpressed in Escherichia coli and purified to homogeneity. Crystallization experiments yielded crystals that were suitable for high-resolution X-ray diffraction analysis.


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The expression, purification and crystallization of S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, an essential enzyme from the folate-biosynthesis pathway, is reported.

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The expression, purification and crystallization of nosiheptide-resistance methyltransferase (NSR) from Streptomyces actuosus is described.

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The expression, purification and crystallization of Plasmodium actin-depolymerization factors 1 and 2 are described. X-ray diffraction data were collected to 2.0 and 2.1 Å resolution, respectively, and the structures of both proteins in solution were characterized.

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The expression, purification and crystallization of the periplasmic protein AlgX from P. aeruginosa is described. The crystals diffracted to 2.1 Å resolution.

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Champedak mannose-binding lectin was crystallized at 293 K. Crystallization conditions and preliminary X-ray diffraction analysis are reported.

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Rabbit muscle aldolase (RMA) was crystallized in complex with the low-complexity domain (LC4) of sorting nexin 9. Monoclinic crystals were obtained at room temperature that displayed large mosaicity and poor X-ray diffraction. However, orthorhombic RMA–LC4 crystals grown at 277 K under similar conditions exhibited low mosaicity, allowing data collection to 2.2 Å Bragg spacing and structure determination.

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The cloning, purification, crystallization and preliminary crystallographic studies of three DsbA-like proteins present in S. enterica serovar Typhimurium, SeDsbA, SeDsbL and SeSrgA, are reported.

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Diffraction-quality crystals of I. hospitalis neelaredoxin have been produced. The cloning, expression, purification, crystallization and X-ray crystallographic analysis are reported.

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To determine the binding mechanism of BoNT/OFD05 and its ganglioside receptors on neuronal cells, recombinant BoNT/OFD05 receptor-binding domain has been expressed, purified and crystallized.

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Crystallization and preliminary X-ray crystallographic analysis of the tetracycline-degrading monooxygenase TetX2 from B. thetaiotaomicron are reported.

laboratory communications


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A simple `melt test' to distinguish salt crystals from macromolecule crystals is described.
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