Quantitative Imaging of Single, Unstained Viruses with Coherent X-rays

TL;DR

This paper demonstrates the first successful recording and reconstruction of X-ray diffraction patterns from single, unstained viruses, enabling detailed visualization of viral structures and advancing the potential for imaging individual macromolecules.

Contribution

It introduces a novel method for quantitative X-ray imaging of single viruses without staining, paving the way for imaging various biological specimens at the molecular level.

Findings

First X-ray diffraction pattern from a single unstained virus

Visualization of viral capsid structure inside a virion

Method transferable to X-ray free electron lasers

Abstract

Since Perutz, Kendrew and colleagues unveiled the structure of hemoglobin and myoglobin based on X-ray diffraction analysis in the 1950s, X-ray crystallography has become the primary methodology used to determine the 3D structure of macromolecules. However, biological specimens such as cells, organelles, viruses and many important macromolecules are difficult or impossible to crystallize, and hence their structures are not accessible by crystallography. Here we report, for the first time, the recording and reconstruction of X-ray diffraction patterns from single, unstained viruses. The structure of the viral capsid inside a virion was visualized. This work opens the door for quantitative X-ray imaging of a broad range of specimens from protein machineries, viruses and organelles to whole cells. Moreover, our experiment is directly transferable to the use of X-ray free electron lasers, and represents a major experimental milestone towards the X-ray imaging of single macromolecules.