Serial femtosecond crystallography (SFX) is a form of X-ray crystallography developed for use at X-ray free-electron lasers (XFELs).[1][2][3] Single pulses at free-electron lasers are bright enough to generate resolvable Bragg diffraction from sub-micron crystals. However, these pulses also destroy the crystals, meaning that a full data set involves collecting diffraction from many crystals. This method of data collection is referred to as serial, referencing a row of crystals streaming across the X-ray beam, one at a time.
Serial Femtosecond Crystallography (SFX) schematic
^Liu, W.; et al. (2013). "Serial Femtosecond Crystallography of G Protein–Coupled Receptors - PubAg". Science. 342 (6165). US: United States National Agricultural Library: 1521–1524. doi:10.1126/science.1244142. PMC 3902108. PMID 24357322. Retrieved 2019-02-26.
^Mizohata E, Nakane T, Fukuda Y, Nango E, Iwata S (April 2018). "Serial femtosecond crystallography at the SACLA: breakthrough to dynamic structural biology". Biophysical Reviews. 10 (2): 209–218. doi:10.1007/s12551-017-0344-9. PMC 5899704. PMID 29196935.
^Martin-Garcia JM, Conrad CE, Coe J, Roy-Chowdhury S, Fromme P (July 2016). "Serial femtosecond crystallography: A revolution in structural biology". Archives of Biochemistry and Biophysics. 602: 32–47. doi:10.1016/j.abb.2016.03.036. PMC 4909539. PMID 27143509.
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