Serial femtosecond X-ray diffraction of enveloped virus microcrystals

Structural Dynamics
Robert M LawrenceBrenda G Hogue

Abstract

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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Citations

May 5, 2016·Archives of Biochemistry and Biophysics·Jose M Martin-GarciaPetra Fromme
Jul 29, 2016·Journal of Virological Methods·Robert M LawrenceBrenda G Hogue
Jun 20, 2017·Nature Methods·Philip RoedigAlke Meents
Jun 1, 2016·Lab on a Chip·Shuo SuiSarah L Perry
Oct 24, 2017·Reports on Progress in Physics·E A SeddonW Wurth
Oct 17, 2019·The FEBS Journal·Feng-Zhu ZhaoDa-Chuan Yin
Oct 1, 2019·Annual Review of Virology·A Meents, M O Wiedorn

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Methods Mentioned

BETA
X-ray
Assay
electrophoresis
transmission electron microscopy
light
fluorescence microscopy
SANS

Software Mentioned

CrystFEL
MOSFLM

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