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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 19, 2026

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

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

Published on: March 11, 2022

Pink-beam serial crystallography.

A Meents^1,2, M O Wiedorn^3,4, V Srajer⁵

¹Center for Free Electron Laser Science, DESY, Notkestrasse 85, 22607, Hamburg, Germany. alke.meents@desy.de.

Nature Communications

|November 4, 2017

Summary

This summary is machine-generated.

Researchers used pink-beam X-ray pulses to determine protein structures faster than ever before. This new method enables studying rapid biological processes at sub-microsecond timescales.

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$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Related Experiment Videos

Last Updated: Feb 19, 2026

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

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

Published on: March 11, 2022

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

Structural Biology
Biophysics
X-ray Science

Background:

Serial X-ray crystallography enables macromolecular structure determination at X-ray free electron lasers (XFELs) and synchrotron sources.
Current time resolution for serial synchrotron crystallography is limited to millisecond timescales using monochromatic beams.

Purpose of the Study:

To investigate the potential of polychromatic (pink) X-ray beams for time-resolved diffraction experiments at synchrotron sources.
To achieve significantly shorter timescales than previously possible with monochromatic beams.

Main Methods:

Utilized a pink-beam setup with a highly focused, high-photon-flux X-ray pulse (100 ps exposure) per crystal.
Optimized the experimental setup for very low scattering background.
Merged diffraction patterns from numerous small crystals to obtain complete datasets.

Main Results:

Successfully determined the structures of two different protein samples.
Required data from only 50 crystals, a significant reduction compared to monochromatic experiments.
Achieved high-quality diffraction data, demonstrating the method's efficacy.

Conclusions:

Pink-beam serial synchrotron crystallography enables structure determination at sub-microsecond timescales.
This technique significantly enhances the study of rapid, irreversible biological reactions.
High-brightness X-ray facilities can be leveraged for unprecedented time-resolved structural studies.