journal menu
issue contents
May 2018 issue
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
High-resolution crystal structures of closed and open conformations of Mycobacterium smegmatis MabA are reported.
Open 
access
access
Analysing two sequence-related bacterial glycoside hydrolase family 92 mannosidases with distinct functions, a structural basis for their varied specificities is revealed.
Open access
access
A method is presented to simultaneously resolve the crystal symmetry and indexing ambiguity from sparse data sets.
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.
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.
Open access
access
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.
Open access
access
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.
Open access
access
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.
PDB reference: C-terminal domain of doublecortin, 6fnz
Three industrially relevant glucoamylase structures have been determined, revealing how the starch-binding module can adopt different orientations relative to the catalytic domain.
Open access
access
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.
Structures of orthorhombic crystals of lysozyme at pH 4.5 show that the binding of phosphate ions produces long-range conformational changes and that low humidity produces a displacement of the fifth α-helix towards the active-site cavity. The interaction of some anions must be considered when analysing experiments with lysozyme at acidic pH values.
PDB references: lysozyme crystallized in the presence of 100 mM ammonium sulfate at pH 4.5, 6fa0; lysozyme crystallized in the presence of 100 mM lithium sulfate at pH 4.5, 6f9x; lysozyme crystallized in the presence of 10 mM lithium sulfate at pH 4.5, 6f9y; lysozyme crystallized in the presence of 5 mM ammonium sulfate at pH 4.5, 6f9z; lysozyme crystallized in the presence of 100 mM sodium phosphate at pH 4.5, 6f1l; lysozyme crystallized in the presence of 100 mM sodium phosphate at pH 4.5, low-humidity form, 6f1m; orthorhombic lysozyme crystallized at 298 K and pH 4.5, 6f1o; tetragonal lysozyme crystallized at 298 K and pH 4.5 with phosphate bound, 6f1p; tetragonal lysozyme crystallized at 298 K and pH 4.5 with phosphate bound, 6f1r
