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X-ray Crystallography

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...

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Related Experiment Video

Updated: Feb 22, 2026

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.

Tobias Weinert¹, Natacha Olieric¹, Robert Cheng²

¹Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232, Villigen PSI, Switzerland.

Nature Communications

|September 16, 2017

Summary

Room-temperature serial crystallography using synchrotron X-rays is now feasible, enabling structural determination of radiation-sensitive proteins and drug-target interactions without cryo-cooling. This method offers high-quality data comparable to cryo-crystallography.

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Last Updated: Feb 22, 2026

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

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$On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature$

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Cryo-crystallography is standard for mitigating radiation damage in X-ray crystallography.
Radiation damage historically limited room-temperature structure determination.

Purpose of the Study:

To demonstrate the feasibility of room-temperature serial crystallography at synchrotrons.
To showcase its application in determining structures of radiation-sensitive proteins and studying drug interactions.

Main Methods:

Utilized serial millisecond crystallography with a high-viscosity injector and high frame-rate detector at a synchrotron beamline.
Employed a crystal scanning approach for data collection.
Collected 1,000-10,000 diffraction patterns in 3-82 minutes for molecular replacement.

Main Results:

Successfully determined the high-resolution structure of a radiation-sensitive molybdenum storage protein.
Demonstrated colchicine soaking into tubulin and native sulfur phasing of a human G protein-coupled receptor.
Synchrotron data required fewer patterns for de novo phasing compared to free-electron laser data.

Conclusions:

Room-temperature serial crystallography is a viable and routine technique at synchrotrons.
The data quality is comparable to cryo-crystallographic data.
This method expands structural biology capabilities for radiation-sensitive samples and room-temperature experiments.