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The advent and application of the X-ray free-electron laser (XFEL) has uncovered the structures of proteins that could not previously be solved using traditional crystallography. While this new technology is

The advent and application of the X-ray free-electron laser (XFEL) has uncovered the structures of proteins that could not previously be solved using traditional crystallography. While this new technology is powerful, optimization of the process is still needed to improve data quality and analysis efficiency. One area is sample heterogeneity, where variations in crystal size (among other factors) lead to the requirement of large data sets (and thus 10–100 mg of protein) for determining accurate structure factors.

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    Date Created
    • 2015-08-19
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1063/1.4928688
    • Identifier Type
      International standard serial number
      Identifier Value
      2329-7778

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    Abdallah, B. G., Zatsepin, N. A., Roy-Chowdhury, S., Coe, J., Conrad, C. E., Dörner, K., . . . Ros, A. (2015). Microfluidic sorting of protein nanocrystals by size for X-ray free-electron laser diffraction. Structural Dynamics, 2(4), 041719. doi:10.1063/1.4928688

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