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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...

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: Jun 12, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Structural characterization of proteins and complexes using small-angle X-ray solution scattering.

Haydyn D T Mertens¹, Dmitri I Svergun

¹European Molecular Biology Laboratory-Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg, Germany.

Journal of Structural Biology

|June 19, 2010

Summary

This summary is machine-generated.

Small-angle X-ray scattering (SAXS) offers low-resolution structural insights for biological molecules in solution. Advanced SAXS analysis tools now enable rapid characterization of protein solutions, including oligomeric state and quaternary structure.

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Last Updated: Jun 12, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Published on: January 10, 2018

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

Area of Science:

Structural Biology
Biophysics

Background:

Small-angle X-ray scattering (SAXS) is a key technique for characterizing biological macromolecules in solution.
It provides low-resolution three-dimensional structural information.

Purpose of the Study:

To review main approaches for characterizing proteins and protein complexes using SAXS.
To present tools for analyzing proteins in solution.
To discuss the impact of SAXS tools in modern structural biology.

Main Methods:

Utilizes ab initio and rigid body modeling for structure determination.
Assesses oligomeric state and quaternary structure of proteins and complexes.
Complements high-resolution methods like X-ray crystallography and NMR.

Main Results:

SAXS enables quantitative analysis of flexible biological systems.
Current SAXS analysis methods are advanced, allowing automated and rapid characterization.
Provides low-resolution models, quaternary structure, and oligomeric composition of protein solutions.

Conclusions:

SAXS is a powerful and versatile tool for structural biology.
Advanced SAXS analysis has significantly impacted the study of proteins and protein complexes in solution.
The technique is highly complementary to other structural biology methods.