ArticleActa crystallographica. Section D, Biological crystallography2012
X-ray-excited optical luminescence of protein crystals: a new tool for studying radiation damage during diffraction data collection.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Radiation-damage-induced phasing: a case study using UV irradiation with light-emitting diodes.Acta crystallographica. Section D, Structural biology · 2016Article
- In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF.Acta crystallographica. Section D, Biological crystallography · 2015Article
- From protein structure to function via single crystal optical spectroscopy.Frontiers in molecular biosciences · 2015Review
- Real time observation of X-ray-induced surface modification using simultaneous XANES and XEOL-XANES.Analytical chemistry · 2013Article
- A new on-axis micro-spectrophotometer for combining Raman, fluorescence and UV/Vis absorption spectroscopy with macromolecular crystallography at the Swiss Light Source.Journal of synchrotron radiation · 2013Article
- Global radiation damage: temperature dependence, time dependence and how to outrun it.Journal of synchrotron radiation · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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.
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