issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2015 issue

Highlighted illustration

Cover illustration: Structure of RizA, an L-amino-acid ligase from Bacillus subtilis (Kagawa et al., p. 1125).

research communications


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The crystal structure of a 14-3-3ζ–LKB1 fusion protein provides a novel potential binding mode of 14-3-3 to its ligands.

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The potentially structured core domain of the intrinsically disordered protein Knr4, residues 80–340, was expressed and crystallized using native and selenomethionine-labelled proteins.

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The structure of the L-amino-acid ligase RizA was determined at 2.8 Å resolution.

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The middle of syneptonemal complex protein 1, which is composed of a coiled-coil domain, was purified and crystallized. The crystals were found to belong to space group I4, with unit-cell parameters a = 41.95, b = 41.95, c = 318.78 Å. The crystals were obtained at 293 K and diffracted to a resolution of 3.0 Å.

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The crystallization of human kallistatin in the relaxed conformation is reported.


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The Tim50 crystal structure indicates that the IMS domain of Tim50 exhibits significant structural plasticity within the putative presequence-binding groove.

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High-resolution structural analyses of the N-glycosidase ribosome-inactivating protein from seeds of M. charantia show that the enzyme preferentially cleaves nicotinamide from the oxidized form of the coenzyme NADP.

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This article describes preliminary crystallographic data for the I26A/N52A mutant of nonstructural protein 15 from Human coronavirus 229E.

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The actin-polymerizing protein complex Arp2/3 was crystallized in two new space groups. The new electron-density maps from these new crystal forms reveal some details that may help to elucidate how nucleation-promoting factors bind to the complex.

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The crystal structure of the dimerization domain of CEACAM7, a human cell adhesion protein, was determined at 1.47 Å resolution and the Kdimerization was measured by analytical ultracentrifugation.

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The structure of the SPRY domain of the human RNA helicase DDX1 was determined at 2.0 Å resolution. The SPRY domain provides a putative protein–protein interaction platform within DDX1 that differs from other SPRY domains in its structure and conserved regions.

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The six subunits of human prefoldin were overexpressed in E. coli. Prefoldin was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution.

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The subcloning, expression, purification and crystallization of a putative class I labdane-related diterpene synthase identified by genome mining in the genome sequence of a Mexican actinobacterium is reported.

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In this study, a recombinant two-domain laccase from S. griseoflavus was successfully expressed and purified, and crystals were obtained that diffracted to a resolution of 2.0 Å.
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