适用于X射线自由电子激光研究的碳酸酐酶II微晶。
Carbonic anhydrase II microcrystals suitable for XFEL studies.
作者信息
Lomelino Carrie L, Kim Jin Kyun, Lee Cheol, Lim Seon Woo, Andring Jacob T, Mahon Brian P, Chung Moses, Kim Chae Un, McKenna Robert
机构信息
Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Department of Physics, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea.
出版信息
Acta Crystallogr F Struct Biol Commun. 2018 Jun 1;74(Pt 6):327-330. doi: 10.1107/S2053230X18006118. Epub 2018 May 17.
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.
X射线自由电子激光（XFEL）源的最新进展使得对蛋白质动力学的研究成为可能。飞秒X射线脉冲能够可视化酶催化过程中的中间状态。在本研究中，展示了适合在浦项加速器实验室收集XFEL衍射数据的碳酸酐酶II微晶（长度为40 - 80 µm）的生长情况。这些晶体的衍射分辨率达到1.7 Å，并被确定属于空间群P2，晶胞参数为a = 42.2、b = 41.2、c = 72.0 Å，β = 104.2°。这些初步结果为在XFEL光束线进行研究碳酸酐酶催化的时间分辨实验提供了必要的框架。
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