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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

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.

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    Date Created
    • 2015-08-20
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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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