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Carbonic anhydrase II microcrystals suitable for XFEL studies.

Carrie L LomelinoJin Kyun KimCheol LeeSeon Woo LimJacob T AndringBrian P MahonMoses ChungChae Un KimRobert McKenna
Published in: Acta crystallographica. Section F, Structural biology communications (2018)
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.
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