issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

May 2018 issue

Highlighted illustration

Cover illustration: Staggered packings of trigonal protein layers in crystals of the dynamic protein EutL (Thompson et al., p. 411). Left: two unique, but related, packing arrangements obeying P321 symmetry in a crystal composed of oppositely facing layers of trimers (orange cells). Right: partial offset of the threefold symmetry axes in successive layers of the crystal (perpendicular to the hexagonal axis; the a axis here) leads to breakage of trigonal symmetry while preserving monoclinic symmetry (C2, blue cell).

research papers

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Analysing two sequence-related bacterial glycoside hydrolase family 92 mannosidases with distinct functions, a structural basis for their varied specificities is revealed.

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A method is presented to simultaneously resolve the crystal symmetry and indexing ambiguity from sparse data sets.

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Microfocus X-ray data collection from 18 non-overlapping regions of a single protein crystal revealed unit-cell non-isomorphism and subtle protein dynamics across the crystal specimen.

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The high-resolution crystal structure of a Zonocerus variegatus flavin-dependent monooxygenase is reported at 1.6 Å resolution together with kinetic studies of structure-based protein variants in order to investigate significant differences in enzyme activity between isoforms.

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Significant improvements to the sample-location, characterization and data-collection algorithms on the autonomous ESRF beamline MASSIF-1 are described. The workflows now include dynamic beam-diameter adjustment and multi-position and multi-crystal data collections.

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An automated data-processing pipeline for protein microcrystals is presented. The processing of multiple small-wedge data sets was made dramatically easier by this pipeline.

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A large domain swap encompassing half of the molecule is observed in the crystal structure of the C-terminal domain of human doublecortin. Combined with ultracentrifugation data, the domain swap suggests a mechanism by which doublecortin may cooperatively bind and bundle microtubule fibres.

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Three industrially relevant glucoamylase structures have been determined, revealing how the starch-binding module can adopt different orientations relative to the catalytic domain.

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The densities of aqueous solutions of eight common cryoprotectants were measured at T = 77 K and were used to determine electron densities at T = 77 K and thermal contractions on cooling from room temperature. The results provide a quantitative basis for choosing cryoprotectants to optimize outcomes in cryocrystallography, cryo-SAXS, cryogenic temperature X-ray imaging and vitrification-based biological cryopreservation.

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