Related Experiment Video
Updated: Mar 26, 2026

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
Published on: July 20, 2022
Serial femtosecond X-ray diffraction of enveloped virus microcrystals
Robert M Lawrence, Chelsie E Conrad, Nadia A Zatsepin
1Linac Coherent Light Source, SLAC National Accelerator Laboratory , Menlo Park, California 94025, USA.
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.
More Related Videos
Related Concept Videos
X-ray Diffraction of Biological Samples
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are scattered by the electron clouds around the sample atoms. The X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...
Cryo-electron Microscopy
Determination of Crystal Structures

