Destruction-and-diffraction by X-ray free-electron laser.
It is common knowledge that macromolecular crystals are damaged by the X-rays they are exposed to during conventional data collection. One of the claims made about the crystallographic data collection now being collected using X-ray free-electron lasers (XFEL) is that they are unaffected by radiation damage. XFEL data sets are assembled by merging data obtained from a very large number of crystals, each of which is exposed to a single femtosecond pulse of radiation, the duration of which is so short that diffraction occurs before the damage done to the crystal has time to become manifest, i.e. "diffraction-before-destruction." However, recent theoretical studies have shown that many of the elemental electronic processes that ultimately result in the destruction of such crystals occur during a single pulse. It is predicted that the amplitudes of atomic scattering factor could be reduced by as much as 75% within the first 5 femtoseconds of such pulses, and that different atoms will respond in different ways. Experimental evidence is provided here that these predictions are correct.
Department of Molecular Biophysics and Biochemistry, Yale University, Connecticut 06520, New Haven.
Jimin
J
Wang
D003578:Cytochrome-c Peroxidase / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000737:chemistry*; D004583:Electrons; D007834:Lasers; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D000072417:Protein Domains; D012542:Scattering, Radiation
D045332:Photosystem II Protein Complex; D003578:Cytochrome-c Peroxidase; D003576:Electron Transport Complex IV
XFEL; atomic scattering factors; cytochrome c oxidase; cytochrome c peroxidase; metalloproteins; photosystem II; radiation damage