Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@article{Sanishvili2011RadiationDI,
  title={Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.},
  author={Ruslan Sanishvili and Derek W. Yoder and Sudhir Babu Pothineni and Gerd Rosenbaum and Shenglan Xu and Stefan Vogt and Sergey Evgenevich Stepanov and Oleg A. Makarov and Stephen Corcoran and Richard Benn and Venugopalan Nagarajan and Janet L. Smith and Robert F. Fischetti},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 15},
  pages={
          6127-32
        }
}
Radiation damage is a major limitation in crystallography of biological macromolecules, even for cryocooled samples, and is particularly acute in microdiffraction. For the X-ray energies most commonly used for protein crystallography at synchrotron sources, photoelectrons are the predominant source of radiation damage. If the beam size is small relative to the photoelectron path length, then the photoelectron may escape the beam footprint, resulting in less damage in the illuminated volume… CONTINUE READING

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