| Literature DB >> 29870015 |
Carrie L Lomelino1, Jin Kyun Kim2, Cheol Lee2, Seon Woo Lim2, Jacob T Andring1, Brian P Mahon1, Moses Chung2, Chae Un Kim2, Robert McKenna1.
Abstract
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 P21, 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.Entities:
Keywords: X-ray free-electron lasers; XFELs; carbonic anhydrase II; microcrystals; serial femtosecond crystallography; time-resolved crystallography
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Year: 2018 PMID: 29870015 PMCID: PMC5987739 DOI: 10.1107/S2053230X18006118
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056