XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.
Acta Crystallogr D Struct Biol
; 80(Pt 3): 194-202, 2024 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-38411550
ABSTRACT
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 CO2 and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Anidrase Carbônica II
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Estados Unidos