Journal Article

PUBDB-2026-01804

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Cefdinir binding to a class A β-lactamase revealed by serial cryo-crystallography

Gore, G. ; Prester, A. ; Bartels, K. ; von Stetten, D.Extern*EMBL* ; Schulz, E. (Corresponding author)Extern*

2026
Wiley Bognor Regis

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Please use a persistent id in citations: doi:10.1107/S2059798326003992  doi:10.3204/PUBDB-2026-01804

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.Keywords: serial crystallography; CTX-M-14; cefdinir; cephalosporins; antibiotic resistance.

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Contributing Institute(s):

1. Forschungsgruppe für strukturelle Dynamik (MPSD)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)
2. DFG project G:(GEPRIS)458246365 - Zeitaufgelöste Strukturanalysde der extended spectrum Beta-Lactamase CTX-M-14 (458246365) (458246365)
3. DynaPLIX - Dynamics of Protein–Ligand Interactions (101071843) (101071843)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2026

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Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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