XFELs outrun radiation damage with pulses lasting tens of femtoseconds and thereby enable “diffraction before destruction” to solve such protein structures. As the crystals are destroyed by the extremely intense XFEL pulse (after producing a useful diffraction pattern), the sample must be very rapidly replenished in order to collect a full dataset in a reasonable amount of time. Smaller crystals grow more readily from these complex proteins and feature a low degree of long range disorder yet are damaged by the X-ray radiation dose required to collect full, high-resolution datasets using conventional methods. XFELs were proposed to facilitate structural studies of difficult-to-crystallize proteins that failed to produce crystals large enough for traditional synchrotron-based crystallography where the crystal is exposed to the X-ray beam for durations longer than the onset of detrimental radiation damage.
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