In 1912, Max von Laue and collaborators first observed diffraction spots from a millimeter-sized crystal of copper sulfate using an X-ray tube. Crystallography was born of this experiment, and since then, diffraction by both X-rays and electrons has revealed a myriad of inorganic and organic structures, including structures of complex protein assemblies. Advancements in X-ray sources have spurred a revolution in structure determination, facilitated by the development of new methods. This review explores some of the frontier methods that are shaping the future of X-ray diffraction, including coherent diffractive imaging, serial femtosecond X-ray crystallography and small-angle X-ray scattering. Collectively, these methods expand the current limits of structure determination in biological systems across multiple length and time scales.

中文翻译：

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用于高分辨率结构测定的相干 X 射线衍射的前沿方法

1912 年，Max von Laue 和合作者首次使用 X 射线管从毫米大小的硫酸铜晶体中观察到衍射点。晶体学诞生于这个实验，从那时起，X 射线和电子的衍射揭示了无数无机和有机结构，包括复杂蛋白质组装体的结构。X 射线源的进步推动了结构测定的革命，新方法的发展推动了这一革命。本综述探讨了塑造 X 射线衍射未来的一些前沿方法，包括相干衍射成像、串行飞秒 X 射线晶体学和小角 X 射线散射。总的来说，这些方法在多个长度和时间尺度上扩展了生物系统中结构确定的当前限制。