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Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of

Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of “diffraction-before-destruction.” However, de novo structure factor phase determination using XFELs has been difficult so far. We demonstrate the ability to solve the crystallographic phase problem for SFX data collected with an XFEL using the anomalous signal from native sulfur atoms, leading to a bias-free room temperature structure of the human A[subscript 2A] adenosine receptor at 1.9 Å resolution. The advancement was made possible by recent improvements in SFX data analysis and the design of injectors and delivery media for streaming hydrated microcrystals. This general method should accelerate structural studies of novel difficult-to-crystallize macromolecules and their complexes.
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    Title
    • Native phasing of x-ray free-electron laser data for a G protein–coupled receptor
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    Date Created
    2016-09-23
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1126/sciadv.1600292
    • Identifier Type
      International standard serial number
      Identifier Value
      2375-2548

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    Batyuk, A., Galli, L., Ishchenko, A., Han, G. W., Gati, C., Popov, P. A., . . . Cherezov, V. (2016). Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Science Advances, 2(9). doi:10.1126/sciadv.1600292

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