issue contents

ISSN: 2053-230X

December 2016 issue

Highlighted illustration

Cover illustration: The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution (Cala et al., p. 885).

research communications

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The structure of the A. gambiae serine proteinase inhibitor (serpin) SRPN18 was determined, revealing an unusually short and constricted reactive-center loop.

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The crystal structure of Msmeg_6760 reveals a novel fold for a toxin that harbors a large central cavity that is likely to bind a large hydrophobic compound.

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A cellulase from K. pneumoniae was cloned, expressed, purified and shown to be an endoglucanase. Its structure was determined at 1.76 Å resolution and comparisons with homologous enzymes provide information on substrate specificity.

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The cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate reductase from the human-pathogenic bacterium B. henselae, the causative bacterium of cat-scratch disease, are reported.

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FapF from Pseudomonas facilitates the secretion of the amyloid-forming polypeptide FapC across the bacterial outer membrane. A protocol for forming reproducible well diffracting crystals is described in which the switch to tetraethylene glycol monooctyl ether detergent during purification proved to be critical and represents a handy tip for β-barrel protein crystallography.

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A hemihedral twinning problem was found in crystals of a tetrahydrofolate-dependent O-demethylase, LigM, from Sphingobium sp. SYK-6. The problem was overcome using microseeding.

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The high-resolution (1.57 Å) structure and kinetic data of the key fire blight phosphatase AmsI are reported.

addenda and errata

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