Abstract
It is now possible to solve protein structures with femtosecond X-ray free-electron laser (XFEL) pulses that were previously inaccessible to continuous synchrotron sources due to radiation damage. The key to this success is that diffraction probes the protein structure on femtosecond timescales, whereas nuclear motion takes tens to hundreds of femtoseconds to have a significant effect on the crystal structure. This is the essential idea behind the diffraction-before-destruction principle that underlies serial femtosecond crystallography (SFX) with XFELs. In practice, the principle works well enough to determine protein structures of comparable resolution to synchrotron protein crystallography, which has led to the many successes of XFEL crystallography to date.
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