Carbonic anhydrase II microcrystals suitable for XFEL studies.

Citation data:

Acta crystallographica. Section F, Structural biology communications, ISSN: 2053-230X, Vol: 74, Issue: Pt 6, Page: 327-330

Publication Year:
2018
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Repository URL:
http://scholarworks.unist.ac.kr/handle/201301/24178
PMID:
29870015
DOI:
10.1107/s2053230x18006118
Author(s):
Lomelino, Carrie L; Kim, Jin Kyun; Lee, Cheol; Lim, Seon Woo; Andring, Jacob T; Mahon, Brian P; Chung, Moses; Kim, Chae Un; McKenna, Robert
Publisher(s):
International Union of Crystallography (IUCr); International Union of Crystallography; INT UNION CRYSTALLOGRAPHY
Tags:
Biochemistry, Genetics and Molecular Biology; Physics and Astronomy; X-ray free-electron lasers; XFELs; serial femtosecond crystallography; time-resolved crystallography; microcrystals; carbonic anhydrase II.
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article description
Recent advances in X-ray free-electron laser (XFEL) sources have permitted the study of protein dynamics. Femtosecond X-ray pulses have allowed the visualization of intermediate states in enzyme catalysis. In this study, the growth of carbonic anhydrase II microcrystals (40-80 µm in length) suitable for the collection of XFEL diffraction data at the Pohang Accelerator Laboratory is demonstrated. The crystals diffracted to 1.7 Å resolution and were indexed in space group P2, with unit-cell parameters a = 42.2, b = 41.2, c = 72.0 Å, β = 104.2°. These preliminary results provide the necessary framework for time-resolved experiments to study carbonic anhydrase catalysis at XFEL beamlines.