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YouTube video by International Union of Crystallography

YouTube video by International Union of Crystallography

Crystal structures of the poly-γ-glutamate hydrolase from bacteriophage PM1 were determined in both apo and zinc-bound forms, revealing for the first time a zinc-activated water molecule positioned for nucleophilic attack at the catalytic center. This observation supports a zinc-dependent, water-mediated catalytic mechanism for phage-encoded poly-γ-glutamate hydrolases implicated in loss of viscosity in natto fermentation.

Here, we document the generation of a T7 Express ΔcybC strain allowing contaminant-free expression of the anti-BRIL Fab BAG2. We also report the crystal structure of BAG2 in complex with native cytochrome b562, a complex arising from expression in canonical Escherichia coli strains.

High-resolution X-ray structures of carbonic anhydrase II in complex with two 1,3-oxazole-containing sulfonamide inhibitors define the interactions responsible for their exceptional inhibitory potency and reveal how subtle ligand instability can influence electron-density interpretation and model refinement.