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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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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...

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Related Experiment Video

Updated: Nov 22, 2025

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

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

Published on: March 11, 2022

Macromolecular room temperature crystallography.

Marcus Fischer^1,2

¹Department of Chemical Biology & Therapeutics, St. Jude Children's Research Hospital, Memphis, TN38105, USA.

Quarterly Reviews of Biophysics

|January 8, 2021

Summary

This summary is machine-generated.

Collecting X-ray crystallography data at room temperature (RT) reveals crucial protein conformations often missed at cryogenic temperatures. This review simplifies RT data collection, enabling deeper insights into protein dynamics for research and medicine.

Keywords:

Cryogenic trapping X-ray crystallography energy landscape room temperature structural dynamics variable temperature

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Last Updated: Nov 22, 2025

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

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Author Spotlight: Advancing Protein Structure Analysis for Drug Development

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Published on: March 8, 2024

Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

X-ray crystallography is vital for understanding protein structure and function.
Cryogenic temperature experiments offer practical advantages but may obscure functionally relevant protein conformations.
Alternative protein conformations are often only observable at room temperature (RT).

Purpose of the Study:

To demystify the practical challenges of collecting X-ray crystallography data at room temperature (RT).
To encourage routine RT data collection at synchrotron sources.
To highlight the utility of RT data for exploring protein conformational landscapes.

Main Methods:

Review of practical aspects for preparing, acquiring, and analyzing X-ray crystallography data at RT.
Presentation of conceptual and experimental templates for RT-inspired studies.
Discussion of strategies to overcome perceived impracticalities of RT data collection.

Main Results:

RT X-ray crystallography can reveal functionally important alternative protein conformations.
Practical guidance and examples are provided to facilitate RT data collection.
RT data collection offers diverse and novel insights into protein conformational dynamics.

Conclusions:

Routine X-ray crystallography data collection at RT is feasible and beneficial.
RT studies enhance our understanding of protein conformational landscapes.
An integrative view of protein dynamics at RT advances basic and biomedical research.