Center for Free Electron Laser Science, DESY, Notkestrasse 85, 22607, Hamburg, Germany.
Deutsches Elektronen Synchrotron (DESY), Photon Science, Notkestrasse 85, 22607, Hamburg, Germany.
Nat Commun. 2017 Nov 3;8(1):1281. doi: 10.1038/s41467-017-01417-3.
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.
连续 X 射线晶体学允许在 X 射线自由电子激光器 (XFEL) 和最近的同步加速器源上进行大分子结构测定。连续同步加速器晶体学实验的时间分辨率受到单色光束的限制，仅达到毫秒级。多色的“粉色”光束提供了超过两个数量级的光子通量增加，因此允许在同步加速器源的衍射实验中访问更短的时间尺度。在这里，我们通过合并来自许多晶体的粉色光束衍射图案来报告两种不同蛋白质样品的结构测定，每个晶体仅使用优化用于非常低散射背景的设置采集单个 100 ps X 射线脉冲曝光。与单色辐射实验相比，仅需 50 个晶体即可获得完整的数据集。衍射数据的高质量突出了该方法在使用高亮度 X 射线设施研究亚微秒时间尺度的不可逆反应方面的潜力。
