Pink-beam serial crystallography
Pink-beam serial crystallography
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DOI：
10.1038/s41467-017-01417-3
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发表时间：
2017-11-03
影响因子：
16.6
通讯作者：
Chapman, H. N.
中科院分区：
文献类型：
--
作者：
Meents, A.;Wiedorn, M. O.;Chapman, H. N.
串行 X 射线晶体学可以在 X 射线自由电子激光器 (XFEL) 和最近的同步加速器源上测定大分子结构。串行同步加速器晶体学实验的时间分辨率仅限于单色光束的毫秒时间尺度。多色“粉红色”光束提供了超过两个数量级的增加的光子通量，因此允许在同步加速器源的衍射实验中获得更短的时间尺度。在这里，我们报告了通过合并来自许多晶体的粉红色光束衍射图案来确定两种不同蛋白质样品的结构，每个晶体使用针对极低散射背景优化的设置，通过每个晶体的单个 100 ps X 射线脉冲曝光来收集每个样品。与单色辐射实验相比，只需 50 个晶体的数据即可获得完整的数据集。高质量的衍射数据凸显了该方法使用高亮度 X 射线设备研究亚微秒时间尺度不可逆反应的潜力。
Serial X-ray crystallography allows macromolecular structure determination at both X-ray free electron lasers (XFELs) and, more recently, synchrotron sources. The time resolution for serial synchrotron crystallography experiments has been limited to millisecond timescales with monochromatic beams. The polychromatic, "pink", beam provides a more than two orders of magnitude increased photon flux and hence allows accessing much shorter timescales in diffraction experiments at synchrotron sources. Here we report the structure determination of two different protein samples by merging pink-beam diffraction patterns from many crystals, each collected with a single 100 ps X-ray pulse exposure per crystal using a setup optimized for very low scattering background. In contrast to experiments with monochromatic radiation, data from only 50 crystals were required to obtain complete datasets. The high quality of the diffraction data highlights the potential of this method for studying irreversible reactions at sub-microsecond timescales using high-brightness X-ray facilities.