issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2018 issue

Highlighted illustration

Cover illustration: Structural characterization of enoyl-ACP reductase II (FabK) from Porphyromonas gingivalis, a `keystone' species in periodontal disease (Hevener et al., p. 105).

research communications



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In order to study the oligomeric structure of human CCL5, a new strategy to prepare the CCL5 trimer was developed and a crystal was obtained that diffracted to a satisfactory resolution of 1.87 Å.

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The oligomeric state of the 2-Cys peroxiredoxin from the green alga Chlamydomonas reinhardtii was determined by an X-ray crystallographic study and high-speed AFM image analysis.

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Although the enzymatic activity of cytochrome c oxidase (CcO) depends sensitively on pH over a wide range, X-ray structural analyses of bovine CcO have been conducted using crystals prepared at pH 5.7 owing to the difficulty in crystallizing this protein. Here, the structure of ligand-free reduced CcO was successfully determined at 1.99 Å resolution.

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Ribokinase from L. donovani was cloned, purified, characterized and crystallized, and data were collected to a resolution of 1.95 Å. X-ray crystallographic analysis showed the presence of two molecules in the asymmetric unit, and human ribokinase could be used as a template to determine the three-dimensional structure.

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The structure of Porphyromonas gingivalis enoyl-ACP reductase II (FabK) was determined via X-ray crystallography to 1.9 Å resolution with all flexible loops visible, FMN fully resolved and the NADPH cofactor partially resolved. Characterization includes the structural basis of NADPH dependence and the role of a required monovalent cation.

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Cellulosomes are capable of efficiently degrading cellulosic biomass. Crystallization and diffraction analysis of xylanase, which is part of the multi-enzyme cellulosome of Clostridium cellulovorans 743B, are reported.

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Purification, crystallization and X-ray crystallographic analysis were employed to determine the catalytic mechanism of Est8, a GDSL-motif esterase from Bacillus sp. K91.
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