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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 13, 2026

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

Where is crystallography going?

Jonathan M Grimes¹, David R Hall¹, Alun W Ashton¹

¹Science Division, Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, England.

Acta Crystallographica. Section D, Structural Biology

|March 14, 2018

Summary

This summary is machine-generated.

Macromolecular crystallography (MX) remains a vital tool in biology, continually advancing with new technologies like synchrotron radiation and X-ray free-electron lasers. The field is evolving to address whether emerging electron imaging methods will supersede traditional X-ray techniques.

Keywords:

XFELs electron diffraction electron microscopy macromolecular crystallography synchrotrons

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Last Updated: Feb 13, 2026

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Published on: July 6, 2019

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Published on: June 5, 2021

Area of Science:

Structural biology
Biophysics
Biochemistry

Background:

Macromolecular crystallography (MX) has been a cornerstone of biological research for over 50 years.
Revolutions in recombinant protein production and cryo-crystallography have significantly expanded MX's capabilities.
Advances in synchrotron radiation, including detectors, optics, and automation, have driven progress over the last three decades.

Purpose of the Study:

To assess the current health and future prospects of macromolecular crystallography.
To compare the advantages and limitations of MX against emerging electron imaging techniques.
To provide insights into the ongoing evolution of structural biology methods.

Main Methods:

Review of historical advancements in macromolecular crystallography.
Discussion of current and emerging technologies such as synchrotron radiation and X-ray free-electron lasers.
Comparative analysis with single-particle electron microscopy and electron diffraction.

Main Results:

Synchrotron radiation has led to significant improvements in signal-to-noise ratios for X-ray experiments.
X-ray free-electron lasers enable studies of protein dynamics at the subpicosecond timescale without radiation damage.
Emerging electron imaging methods present potential challenges and alternatives to traditional MX.

Conclusions:

Macromolecular crystallography continues to evolve and offer unique advantages in structural biology.
The field must adapt to and integrate new technologies to maintain its leading role.
The future likely involves a synergistic approach combining X-ray and electron-based imaging methods.