issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

October 2016 issue

Highlighted illustration

Cover illustration: The structure of glycoside hydrolase 29 family member GH29_0940, a protein cloned from metagenomic DNA from the rumen of a cow, reveals unique dual carbohydrate-binding domains (Summers et al., p. 750).

research communications


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The dimeric structure of the C-terminal domain of Grx6, bridged by one [2Fe–2S] cluster coordinated by the active-site Cys136 and two external glutathione molecules, is reported.

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The purification, crystallization and X-ray diffraction analysis of the Arabidopsis receptor-like cytoplasmic kinase BIK1, which plays an important role in growth and immune signaling pathways, are described.

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The crystal structure of mouse phospholipid hydroperoxide glutathione peroxidase 4 solved at 1.8 Å resolution and the first solution structural studies of a glutathione peroxidase protein are reported.

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A high-resolution crystal structure of an unknown glycoside hydrolase enzyme from the rumen of B. taurus is presented. Unique dual carbohydrate-binding domains are revealed.

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Microgravity was used in an attempt to define the crystal structure of the polyQ repeat of huntingtin alone or bound to MW1, an anti-polyQ Fab. While huntingtin was not crystallized in the experiments, analysis of microgravity-grown and Earth-grown MW1 Fab crystals showed that, on average, microgravity-grown crystals of MW1 Fab showed an increase in size and an improvement in resolution and mosaicity when compared with Earth-grown crystals in one space group, in agreement with data published for other proteins, although the highest overall resolution X-ray data in our experiments were obtained from a crystal grown on Earth.

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New crystallization conditions were identified that allowed the structure determination of human cyclooxygenase-2 in complex with rofecoxib (Vioxx) and the structure was subsequently determined to 2.7 Å resolution.

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TtuA and TtuB are the sulfur transferase and sulfur carriers for the biosynthesis of 2-thioribothymidine in some bacterial tRNAs. To elucidate their mechanism of interaction, the TtuA–TtuB complex from T. thermophilus was crystallized and a Zn-MAD data set was collected to a resolution of 2.5 Å.

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The extracellular domain of the A. thaliana ATP receptor DORN1 has been expressed and purified; a protein orthologous to DORN1 from C. sativa has been crystallized and its X-ray diffraction data have been collected.

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Crystals of the multicopper oxidase CueO obtained from a perdeuterated sample for neutron diffraction diffracted to 1.8 Å resolution using X-rays and their crystal structure was solved.

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The GDP-D-mannose pyrophosphorylase VTC1 from A. thaliana was crystallized and co-crystallized with its substrate. X-ray diffraction data were collected for crystallographic analysis.
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