Femtosecond X-ray diffraction from two-dimensional protein crystals.
Femtosecond X-ray diffraction from two-dimensional protein crystals.
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DOI：
10.1107/s2052252514001444
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发表时间：
2014-03-01
期刊：
影响因子：
3.9
通讯作者：
Evans JE
中科院分区：
文献类型：
--
作者：
Frank M;Carlson DB;Hunter MS;Williams GJ;Messerschmidt M;Zatsepin NA;Barty A;Benner WH;Chu K;Graf AT;Hau-Riege SP;Kirian RA;Padeste C;Pardini T;Pedrini B;Segelke B;Seibert MM;Spence JC;Tsai CJ;Lane SM;Li XD;Schertler G;Boutet S;Coleman M;Evans JE
介绍了使用飞秒X射线激光快照从二维蛋白质晶体中实现的布拉格衍射。本文介绍了利用X射线自由电子激光器（XFEL）产生的飞秒X射线脉冲获得的二维（2-D）蛋白质晶体的X射线衍射图。迄今为止，由于辐射损伤，还不可能从单个2-D蛋白质晶体获得透射X射线衍射图案。然而，XFEL产生的强烈和超快脉冲允许在样品被破坏之前收集衍射数据的新方法。利用在直线加速器相干光源处的破坏前衍射方法，对于两个不同的2-D蛋白质晶体样品，每个样品小于10 nm厚并保持在室温下，获得优于8.5 nm分辨率的布拉格衍射。 这些原理证明的结果表明，作为2-D晶体排列的可溶性和膜蛋白的结构分析，而不需要低温条件或形成三维晶体的承诺。
Bragg diffraction achieved from two-dimensional protein crystals using femtosecond X-ray laser snapshots is presented. X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.