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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

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 Crystallography02:18

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...
Determination of Crystal Structures01:29

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: Jun 21, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

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

Published on: November 5, 2018

Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS).

Greg L Hura1, Angeli L Menon, Michal Hammel

  • 1Physical Bioscience Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA.

Nature Methods
|July 22, 2009
PubMed
Summary
This summary is machine-generated.

We developed an efficient high-throughput pipeline for analyzing protein structures in solution using small angle X-ray scattering (SAXS). This method rapidly characterizes protein oligomeric states and shapes, advancing structural genomics research.

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

Related Experiment Videos

Last Updated: Jun 21, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

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
09:15

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

Published on: January 10, 2018

Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Understanding protein structure in solution is crucial for biological function.
  • High-throughput methods are needed to accelerate structural genomics.
  • Small angle X-ray scattering (SAXS) provides low-resolution structural information.

Purpose of the Study:

  • To present an efficient pipeline for high-throughput analysis of protein structure in solution using SAXS.
  • To automate sample handling, data collection, and analysis for SAXS experiments.
  • To assess the pipeline's capability in characterizing protein oligomeric states and structures.

Main Methods:

  • Automated sample handling of microliter volumes.
  • Temperature and anaerobic control during data collection.
  • Rapid data collection and analysis coupled with automated archiving.
  • Application of the pipeline to 50 representative proteins.

Main Results:

  • Successfully analyzed 50 proteins, identifying 30 as multimeric structures in solution.
  • Distinguished aggregated and unfolded proteins, defined global structural parameters, and determined oligomeric states.
  • Identified shapes and similar structures for 25 unknown proteins and determined envelopes for 41 proteins.

Conclusions:

  • The developed high-throughput SAXS pipeline is efficient and effective for protein structure analysis in solution.
  • This technology can significantly accelerate structural genomics research.
  • The pipeline enables rapid characterization of protein oligomeric states, structures, and shapes.