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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

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 crystal...

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Determination of Crystal Structures

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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Related Experiment Video

Updated: May 30, 2026

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

X-ray crystallography.

Lauren E Roth¹, F Akif Tezcan

¹Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92037, USA. leroth@ucsd.edu

Methods in Molecular Biology (Clifton, N.J.)

|August 12, 2011

Summary

This summary is machine-generated.

X-ray crystallography reveals detailed structures of nitrogenase enzymes, crucial for understanding their function. This guide focuses on crystallizing and determining structures of nitrogenase proteins from Azotobacter vinelandii.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Last Updated: May 30, 2026

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

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Published on: April 24, 2018

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

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Published on: March 11, 2022

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

Nitrogenase is a key enzyme in nitrogen fixation.
X-ray crystallography provides high-resolution structural insights into nitrogenase.
Understanding nitrogenase structure is vital for its functional studies.

Purpose of the Study:

To guide researchers in crystallizing nitrogenase component proteins.
To detail methods for determining nitrogenase structures.
To highlight the importance of X-ray crystallography for nitrogenase research.

Main Methods:

X-ray crystallography techniques.
Protein crystallization procedures.
Structure determination protocols.

Main Results:

Established methods for crystallizing nitrogenase component proteins.
High-resolution structural models of nitrogenase.
Insights into metal clusters and nucleotide binding.

Conclusions:

X-ray crystallography is essential for advancing nitrogenase research.
Detailed structural information aids in understanding enzyme mechanisms.
Focus on Azotobacter vinelandii provides a robust framework for future studies.