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김채운

Kim, Chae Un
High Pressure X-ray Science Lab.
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XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures

Author(s)
Hull, Joshua A.Lee, CheolKim, Jin KyunLim, Seon WooPark, JaehyunPark, SehanLee, Sang JaePark, GisuEom, IntaeKim, MinseokHyun, HyoJungCombs, Jacob E.Andring, Jacob T.Lomelino, CarrieKim, Chae UnMcKenna, Robert
Issued Date
2024-03
DOI
10.1107/S2059798324000482
URI
https://scholarworks.unist.ac.kr/handle/201301/82638
Citation
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.80, no.3, pp.194 - 202
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.
Publisher
INT UNION CRYSTALLOGRAPHY
ISSN
2059-7983
Keyword (Author)
X-ray crystallographyNMRcarbonic anhydrase IIXFELsneutron diffraction crystallographyradiation damage
Keyword
CRYSTALLOGRAPHYMECHANISMDIOXIDERADIATION-DAMAGEACTIVE-SITE

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