Description

About 2.5 × 10[superscript 6] 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

About 2.5 × 10[superscript 6] 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.

Reuse Permissions
  • application/pdf

    Download count: 0

    Details

    Contributors
    Date Created
    • 2015-05-15
    Resource Type
  • Text
  • Collections this item is in
    Identifier
    • Digital object identifier: 10.1063/1.4919903
    • Identifier Type
      International standard serial number
      Identifier Value
      2329-7778
    Note

    Citation and reuse

    Cite this item

    This is a suggested citation. Consult the appropriate style guide for specific citation guidelines.

    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

    Machine-readable links