This article describes the structural characterization of the class IIIb chitinase from Crocus vernus bulbs. Antifungal and chitinase assays have also been performed to evaluate the potential of the enzyme.

In its wild-type form, the flexible two-domain protein InlB392 yielded poorly reproducible crystals that diffracted to low resolution. Single surface substitutions to tyrosine (T336Y) or glutamate (V333E) yielded well diffracting crystals, suggesting that surface properties, rather than interdomain flexibility, might be the primary impediment to crystallization of the wild type.

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.

This study advances our understanding of pteridine glycosylation and also provides a structural basis for investigating photosynthetic signaling pathways in cyanobacteria.

This 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+.

CryoSift 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.

A high-resolution X-ray structure of a Gln143Asn variant of manganese superoxide dismutase (MnSOD) reveals multiple hydrogen peroxide-binding sites beyond the canonical LIG and PEO binding positions within the active site. These findings expand the known landscape of product peroxide-bound states in MnSOD.

We present the first detailed structure of a newly discovered fucosidase that has been shown to remove terminal fucose from fucoidan, uncovering unique features that set it apart from other known fucosidases and suggesting functional diversity among its homologs.

Mouse ketohexokinase A undergoes a conformational change during the catalytic cycle. The conformational change is consistent between the two isozymes, A and C, and across species.