XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.
NMR
X-ray crystallography
XFELs
carbonic anhydrase II
neutron diffraction crystallography
radiation damage
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Mar 2024
01 Mar 2024
Historique:
medline:
27
2
2024
pubmed:
27
2
2024
entrez:
27
2
2024
Statut:
aheadofprint
Résumé
The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO
Identifiants
pubmed: 38411550
pii: S2059798324000482
doi: 10.1107/S2059798324000482
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Research Foundation of Korea
ID : 2022R1A2C2091815