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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...

$X-ray Diffraction of Biological Samples$ 01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
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...

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Related Experiment Video

Updated: Feb 22, 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

Structure determination based on continuous diffraction from macromolecular crystals.

Henry N Chapman¹, Petra Fromme²

¹Center for Free-Electron Laser Science, DESY, 22607 Hamburg, Germany; Department of Physics, University of Hamburg, 22761 Hamburg, Germany; Center for Ultrafast Imaging, University of Hamburg, 22761 Hamburg, Germany.

Current Opinion in Structural Biology

|September 17, 2017

Summary

This summary is machine-generated.

Researchers developed a new method for single-molecule diffraction using X-ray free-electron lasers. This technique overcomes weak scattering signals, enabling structure determination without crystallization and advancing macromolecular crystallography.

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Related Experiment Videos

Last Updated: Feb 22, 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

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Area of Science:

Structural biology
Biophysics
Crystallography

Background:

Advanced X-ray sources like free-electron lasers (FELs) enable new structural biology techniques.
Single-molecule diffraction is a highly sought-after method to determine macromolecular structures without crystallization.
Traditional crystal diffraction often lacks sufficient data for direct phasing.

Purpose of the Study:

To develop novel methods for single-molecule diffraction using coherent X-ray sources.
To overcome the challenge of weak scattering signals from individual biological molecules.
To enable direct phasing of diffraction data from single biological macromolecules.

Main Methods:

Utilizing coherent diffractive imaging (CDI) principles.
Combining CDI with crystals exhibiting translational disorder.
Collecting continuous femtosecond X-ray diffraction data.

Main Results:

Successfully phased diffraction data from single photosystem II complexes.
Demonstrated a novel approach to single-molecule structure determination.
Overcame limitations of traditional crystallography for phasing.

Conclusions:

The developed method represents a paradigm shift in crystallography.
Enables structure determination of biological macromolecules without crystallization.
Advances the field of single-molecule imaging and structural analysis.