title: X-ray-excited optical luminescence of protein crystals: a new tool for studying radiation damage during diffraction data collection.
abstract: During X-ray irradiation protein crystals radiate energy in the form of small amounts of visible light. This is known as X-ray-excited optical luminescence (XEOL). The XEOL of several proteins and their constituent amino acids has been characterized using the microspectrophotometers at the Swiss Light Source and Diamond Light Source. XEOL arises primarily from aromatic amino acids, but the effects of local environment and quenching within a crystal mean that the XEOL spectrum of a crystal is not the simple sum of the spectra of its constituent parts. Upon repeated exposure to X-rays XEOL spectra decay non-uniformly, suggesting that XEOL is sensitive to site-specific radiation damage. However, rates of XEOL decay were found not to correlate to decays in diffracting power, making XEOL of limited use as a metric for radiation damage to protein crystals.
authors.affiliation: Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, England. robin.owen@diamond.ac.uk
authors.forename: Robin L
authors.initials: RL
authors.lastname: Owen
authors.forename: Briony A
authors.initials: BA
authors.lastname: Yorke
authors.forename: Arwen R
authors.initials: AR
authors.lastname: Pearson
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D001052:Apoferritins / Q000737:chemistry; D002645:Chickens; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D006736:Horses; D049449:Luminescence; D009113:Muramidase / Q000737:chemistry; D007652:Oxo-Acid-Lyases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013820:Thermolysin / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods*; D014965:X-Rays
chemical_list: D000596:Amino Acids; D011506:Proteins; D001052:Apoferritins; C421864:hen egg lysozyme; D009113:Muramidase; D013820:Thermolysin; D007652:Oxo-Acid-Lyases; C018728:N-acetylneuraminate lyase