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Lipidico Injection Protocol for Serial Crystallography Measurements at the Australian Synchrotron

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Virus Structures by X-Ray Free-Electron Lasers.

A Meents¹, M O Wiedorn^1,2

¹Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany;

Annual Review of Virology

|October 1, 2019

Summary

This summary is machine-generated.

X-ray free-electron lasers (XFELs) enable virus structure determination using serial femtosecond crystallography. This method allows room-temperature, non-frozen experiments, overcoming previous limitations.

Keywords:

X-ray free-electron laser XFEL serial crystallography single particle imaging structure determination virus crystallography

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Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

X-ray crystallography has been the primary method for determining virus structures.
Advancements in X-ray sources have led to the development of X-ray free-electron lasers (XFELs).
Traditional methods often require crystal freezing, limiting experimental conditions.

Purpose of the Study:

To explore the application of XFELs for virus structure determination.
To investigate the potential of serial femtosecond crystallography (SFX) for virus studies.
To enable room-temperature and non-equilibrium experiments in virus crystallography.

Main Methods:

Utilizing high-intensity femtosecond X-ray pulses from XFELs.
Employing the diffraction-before-destruction principle to overcome dose limitations.
Applying serial femtosecond crystallography with microcrystals, avoiding cryo-cooling.

Main Results:

XFELs facilitate virus structure determination from single particles at room temperature.
Serial femtosecond crystallography allows structure determination from hundreds to thousands of microcrystals.
Experiments can be performed under non-equilibrium conditions, such as laser-induced temperature jumps or rapid chemical mixing.

Conclusions:

XFELs and SFX offer a powerful new approach to virus structure determination.
This technique overcomes the limitations of traditional cryo-crystallography and electron microscopy.
It opens avenues for studying viruses under biologically relevant, non-equilibrium conditions.