issue contents
December 2025 issue

Cover illustration: Two different orientations of the NAD coenzyme are fortuitously observed in the NAD+-bound structure of a short-chain dehydrogenase from the pathogenic organism Brucella ovis, providing insights into the conformational changes that accompany coenzyme binding [Zupko et al. (2025), Acta Cryst. F81, 487–494].
research communications
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accessThis article describes the structural characterization of a short-chain dehydrogenase from the pathogenic bacterium Brucella ovis. In this manuscript, two structures are described: the structure of the apo protein and a structure containing the coenzyme NAD+.
This study advances our understanding of pteridine glycosylation and also provides a structural basis for investigating photosynthetic signaling pathways in cyanobacteria.
PF1765 from P. furiosus crystallized from a single protein batch in 104 of 192 conditions, yielding ten high-resolution structures (1.1–1.5 Å) across two space groups. Despite wide chemical variability, the overall fold remained nearly identical, with conserved crystal contacts and hydration sites, while subtle lattice-specific rotameric differences highlight the utility of this protein as a model for studying packing effects and microheterogeneity.
methods communications
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accessCryoSift is a CNN-based tool that assesses the quality of 2D class averages. The incorporation of CryoSift into cryoSPARC workflows enables automated particle-stack cleaning.
EMDB reference: mouse apoferritin, EMD-70880

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