ArticleActa crystallographica. Section D, Structural biology2026
Cefdinir binding to a class A β-lactamase revealed by serial cryo-crystallography.
Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
One of the most common resistance mechanisms against antibiotics employed by Gram-negative bacteria involves the production of β-lactamases, resulting in rapid hydrolysis of the antibiotic. Extensive use of the early-generation cephalosporins led to the rise of extended-spectrum β-lactamases such as CTX-Ms. Cefdinir is an extended-spectrum third-generation cephalosporin administered since the late 1990s; despite this, there is no reported 3D structure of the antibiotic bound to any β-lactamase or penicillin-binding protein in the PDB. Here, we report the X-ray crystallographic structure of cefdinir-bound CTX-M-14 E166A mutant obtained via serial cryo-crystallography.
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