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January 2024 issue
Cover illustration: The outer membrane porin OmpW from the pervasive pathogen Klebsiella pneumoniae [Seddon et al. (2024), Acta Cryst. F80, 22–27]. Outer membrane porins are an important class of β-barrel proteins that form water-filled channels in Gram-negative bacteria and, from a clinical perspective, are important in modulating the diffusion of antibiotics into the bacterial cell.
research communications
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High-resolution X-ray crystallography reveals new details of conformational heterogeneity for the dynamic enzyme PTP1B.
PDB reference: PTP1B, 8u1e
The crystal structure of a class A β-lactamase from a clinical strain of Nocardia cyriacigeorgica is reported at high resolution.
PDB reference: class A β-lactamase from Nocardia cyriacigeorgica, 8qnn
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The crystal structure of the outer membrane protein OmpW from Klebsiella pneumoniae is reported.
PDB reference: OmpW from Klebsiella pneumoniae, 8qxp
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