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Determination of Crystal Structures

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In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...

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Updated: Mar 27, 2026

Protein Crystallization for X-ray Crystallography

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Progress in protein crystallography.

Zbigniew Dauter¹, Alexander Wlodawer

¹Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD and Argonne, IL, USA. dauter@anl.gov.

Protein and Peptide Letters

|January 7, 2016

Summary

This summary is machine-generated.

Macromolecular crystallography now uses powerful automated programs to solve complex structures quickly. However, researchers must still validate these results before public release.

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Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

Macromolecular crystallography has advanced significantly from manual methods to highly automated processes.
Modern techniques enable rapid determination of crystal structures for large biological systems.

Purpose of the Study:

To highlight the evolution of macromolecular crystallography.
To emphasize the role of automation and interdisciplinary advances.
To stress the importance of structure validation.

Main Methods:

Leveraging advances in genetic engineering and computer technology.
Utilizing synchrotron beam lines and other sophisticated techniques.
Employing powerful automatic programs for structure determination.

Main Results:

Crystal structures of large macromolecules can now be solved in hours or minutes.
The field has become highly interdisciplinary, integrating multiple scientific domains.
Automation allows for near-human-intervention-free structure solving.

Conclusions:

Contemporary automated systems in macromolecular crystallography are highly effective.
Despite automation, rigorous validation of solved structures is crucial before dissemination.
The interdisciplinary nature of the field drives its continued progress.