Description
Serial femtosecond crystallography (SFX) using X-ray free-electron lasers has produced high-resolution, room temperature, time-resolved protein structures. We report preliminary SFX of Sindbis virus, an enveloped icosahedral RNA virus with ∼700 Å diameter. Microcrystals delivered in viscous agarose medium diffracted to ∼40 Å

Serial femtosecond crystallography (SFX) using X-ray free-electron lasers has produced high-resolution, room temperature, time-resolved protein structures. We report preliminary SFX of Sindbis virus, an enveloped icosahedral RNA virus with ∼700 Å diameter. Microcrystals delivered in viscous agarose medium diffracted to ∼40 Å resolution. Small-angle diffuse X-ray scattering overlaid Bragg peaks and analysis suggests this results from molecular transforms of individual particles. Viral proteins undergo structural changes during entry and infection, which could, in principle, be studied with SFX. This is an important step toward determining room temperature structures from virus microcrystals that may enable time-resolved studies of enveloped viruses.
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    Title
    • Serial femtosecond X-ray diffraction of enveloped virus microcrystals
    Date Created
    2015-08-20
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1063/1.4929410
    • Identifier Type
      International standard serial number
      Identifier Value
      2329-7778

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    Lawrence, R. M., Conrad, C. E., Zatsepin, N. A., Grant, T. D., Liu, H., James, D., . . . Hogue, B. G. (2015). Serial femtosecond X-ray diffraction of enveloped virus microcrystals. Structural Dynamics, 2(4), 041720. doi:10.1063/1.4929410

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