issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

October 2025 issue

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Cover illustration: The crystal structure of Cryptococcus humicola D-aspartate oxidase was determined at 1.70 Å resolution, revealing a unique homotetrameric architecture that distinctly contrasts with the typical dimeric organization of other known D-amino-acid oxidases [Goto et al. (2025), Acta Cryst. F81, 434–440].

SAMPREP


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The focused issue on the SAMPREP workshop is introduced. The virtual issue is available at https://journals.iucr.org/special_issues/2025/samprep23/.

research communications


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The study presented here provides higher resolution data, improved refinement statistics and additional structural details that were previously unresolved in the deposited model of mouse gasdermin D. The structure described in this paper will be valuable to researchers in structural biology, immunology, pharmacology and cell-death mechanisms.

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This report presents the biochemical characterization of phosphorylases from the cyanobacteria Crocosphaera subtropica ATCC 51142 and Synechococcus elongatus PCC 7942, along with preliminary X-ray crystallographic analysis of an isozyme from strain 51142.

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B. subtilis DegQ is a 46-amino-acid regulatory protein involved in the DegS–DegU quorum-sensing system. It folds into a single α-helix, and four monomers assemble into a tetramer characterized by a four-helix coiled-coil structure.

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The crystal structure of Cryptococcus humicola D-aspartate oxidase (chDDO) was determined at 1.70 Å resolution, revealing a unique homotetrameric architecture that distinctly contrasts with the typical dimeric organization of other known D-amino-acid oxidases. This novel oligomerization state is attributed to specific loop insertions and deletions within its FAD-binding and interface domains, facilitating unique inter-subunit interactions, and indicates a distinct substrate-recognition mechanism in chDDO.

methods communications


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PERC (profet, EMPIARreader and CAKED) is a suite of open-source Python software tools facilitating the curation of cryoEM data utilizing standard data-science libraries.
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