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

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Related Experiment Video

Updated: Jun 10, 2026

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collection.

Matthew W Bowler¹, Matias Guijarro, Sebastien Petitdemange

¹Structural Biology Group, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, F-38043 Grenoble, France. bowler@esrf.fr

Acta Crystallographica. Section D, Biological Crystallography

|August 10, 2010

Summary

This summary is machine-generated.

Automated methods and synchrotron facilities are crucial for evaluating biological macromolecule crystal quality. Advanced techniques like microcrystal searching and ordered region selection improve structural biology projects.

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Last Updated: Jun 10, 2026

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

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Published on: July 21, 2017

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Published on: March 15, 2021

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

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Area of Science:

Structural Biology
Crystallography
Biophysics

Background:

Macromolecular crystallography relies on high-quality crystals, but significant variations in diffraction quality are common.
Evaluating numerous samples is standard practice, becoming increasingly critical for complex structural biology projects.

Purpose of the Study:

To present advanced automated methods for evaluating biological macromolecule crystal quality.
To highlight the necessity of synchrotron facilities optimized for high-throughput sample evaluation.

Main Methods:

Development of advanced sample evaluation techniques using micro-focused X-ray beams (5-50 micrometers).
Implementation of methods for searching microcrystals within sample loops and selecting ordered regions in larger crystals.
Creation of a graphical user interface to support these screening methods.

Main Results:

Demonstration of techniques for microcrystal detection and assessment of diffraction-quality heterogeneity within large crystals (diffraction cartography).
Presentation of a user-friendly graphical interface for advanced sample screening.

Conclusions:

Advanced automated sample evaluation is essential for future ambitious structural biology projects.
Synchrotron facilities require upgrades to support high-throughput screening and advanced crystal evaluation techniques.