Serial Femtosecond Crystallography
Serial Femtosecond Crystallography (SFX) is the measurement of crystal structure by rapidly measuring incomplete diffraction patterns from a sequence of identical sample crystals. This is often performed at an XFEL, where a sequence of crystals is dropped through the intense beam. With each snapshot, the crystal is measured shortly before it is destroyed by the intense beam ('diffract-and-destroy'). The sequence of diffraction patterns (slices through the three-dimensional reciprocal-space) can then be merged or analyzed collectively to determine the realspace crystal structure.
As the brightness (high-flux and small spot-size) of modern synchrotrons increase, their measurements of crystals are also approaching the diffract-and-destroy regime; the same reconstruction methods are thus applicable to modern macromolecular crystallography beamlines.
- Chapman et al. Femtosecond X-ray protein nanocrystallography Nature 2011, 470, 73-77. doi: 10.1038/nature09750
- Ilme Schlichting Serial femtosecond crystallography: the first five years IUCrJ 2015, 2 (2). doi: 10.1107/S205225251402702X
- Tao Zhang, Shifeng Jin, Yuanxin Gu, Yao He, Ming Li, Yang Li and Haifu Fan SFX analysis of non-biological polycrystalline samples IUCrJ 2015, 2(3), 322-326. doi: 10.1107/S2052252515002146
- Jörg Standfuss and John Spence Serial crystallography at synchrotrons and X-ray lasers IUCrJ 2017, 4 (2), 100-101. doi: https://doi.org/10.1107/S2052252517001877