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About 2.5 × 106 snapshots on microcrystals of photoactive yellow protein (PYP) from a recent serial femtosecond crystallographic (SFX) experiment were reanalyzed to maximum resolution. The resolution is pushed to 1.46 Å, and a PYP structural model is refined at that

About 2.5 × 106 snapshots on microcrystals of photoactive yellow protein (PYP) from a recent serial femtosecond crystallographic (SFX) experiment were reanalyzed to maximum resolution. The resolution is pushed to 1.46 Å, and a PYP structural model is refined at that resolution. The result is compared to other PYP models determined at atomic resolution around 1 Å and better at the synchrotron. By comparing subtleties such as individual isotropic temperature factors and hydrogen bond lengths, we were able to assess the quality of the SFX data at that resolution. We also show that the determination of anisotropic temperature factor ellipsoids starts to become feasible with the SFX data at resolutions better than 1.5 Å.

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    Title
    • Room Temperature Structures Beyond 1.5 Å by Serial Femtosecond Crystallography
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    Date Created
    2015-05-15
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1063/1.4919903
    • Identifier Type
      International standard serial number
      Identifier Value
      2329-7778
    Note
    • The final version of this article, as published in Structural Dynamics, can be viewed online at: http://aca.scitation.org/doi/10.1063/1.4919903

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    Schmidt, M., Pande, K., Basu, S., & Tenboer, J. (2015). Room temperature structures beyond 1.5 Å by serial femtosecond crystallography. Structural Dynamics, 2(4), 041708. doi:10.1063/1.4919903

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