issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

October 2008 issue

Highlighted illustration

Cover illustration: 6-pyruvoyltetrahydropterin synthase homolog SCO 6650 from Streptomyces coelicolor (Spoonamore et al., p. 875).

protein structure communications


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The X-ray crystal structure of a 6-pyruvoyltetrahydropterin synthase homolog of unknown function has been determined at 1.5 Å resolution. The protein retains residues required for pterin binding, but nearly all catalytic residues are missing.

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Crystals of an E. coli AcrB contaminant were grown from 95% pure CorA preparations. This very frequently occurring problem in membrane-protein crystallography laboratories is reported, as well as suggestions to avoid it.

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The structure and thermal melting data for dehydroquinase from A. fulgidus are reported. The protein melts in vitro well below the organism's growth temperature.

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The crystal structure of apo nicotinic acid mononucleotide adenylyltransferase (NaMNAT) from B. anthracis was determined to 2.3 Å resolution and compared with other bacterial NaMNAT structures.

crystallization communications


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Host–guest complexes of 20S proteasomes with either cytochrome c (cyt c) or green fluorescent protein (GFP) trapped inside the inner cavities of the proteasome have been crystallized. Diffraction data were collected to 3.4 Å (cyt c) and 3.8 Å (GFP) resolution using a synchrotron-radiation source.

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Two types of putative threonyl-tRNA synthetases with complementary functions from the crenarchaea A. pernix K1 and S. tokodaii strain 7 have been overexpressed, purified and crystallized. The crystal structure of one of the four proteins, the catalytic type ThrRS from A. pernix, has successfully been solved by the Se-MAD method.


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S. parahyba chymotrypsin inhibitor in complex with chymotrypsin has been purified and crystallized using the vapour-diffusion method and preliminarily analysis has been performed using X-ray diffraction.

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A novel L-amino-acid oxidase was isolated from V. ammodytes ammodytes venom and crystallized. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. Preliminary diffraction data were collected to 2.6 Å resolution.

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The SET- and RING finger-associated (SRA) domain of human UHRF1 protein has been overexpressed in E. coli, purified and crystallized. The three-dimensional structure of the protein in its SeMet form was solved from 2.2 Å diffraction data using the multiple anomalous dispersion method.

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The crystallization of the HsdR subunit of a putative type I restriction-modification system from V. vulnificus and the collection of diffraction data to 2.6 Å resolution are reported.

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The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from MRSA252 are reported.

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A putative nicotianamine synthase from M. thermoautotrophicus was cloned, expressed, purified and crystallized. The native crystals diffracted to a resolution of 1.7 Å.

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The C-terminal domain of the Methanococcus jannaschii protein MJ0100 includes a CBS-domain pair and has been overexpressed, purified and crystallized. Crystals of selenomethionine-substituted (SeMet) protein were also grown.

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An RNA aptamer in complex with the human IgG Fc fragment have been crystallized. The stirring technique with a rotary shaker was used to improve the crystals and to ensure that they were of high quality and single, resulting in crystals that diffracted to 2.2 Å resolution.

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Recombinant B. pallidus D-arabinose isomerase was crystallized and diffraction data were collected to 2.3 Å resolution.

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The first diffraction-quality crystals of a PutA protein are reported. One of the three crystal forms described here exhibits pseudo-merohedral twinning. Removal of the N-terminal histidine tag aided the crystallization of another form.


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The catalytic domain of an alkaline mannanase from the alkaliphilic Bacillus sp. N16-5 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 combination of leucine-to-methionine substitutions and optimization of cryoconditions improved the resolution of histone chaperone SET/TAF-Iβ/INHAT crystals from around 5.5 to 2.3 Å without changing the crystallization conditions, allowing successful structure determination of SET/TAF-Iβ/INHAT by the multiwavelength anomalous diffraction method.

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The YncE protein of E. coli has been overproduced and purified and preliminary crystallographic analysis has been performed to 2.1 Å resolution. The structure reveals a seven-bladed β-propeller fold.
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