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Related Concept Videos

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...
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...
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...

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Updated: May 14, 2026

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

Published on: January 10, 2018

Developing advanced X-ray scattering methods combined with crystallography and computation.

J Jefferson P Perry1, John A Tainer

  • 1Department of Integrative Structural and Computational Biology and Skaggs, Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA; School of Biotechnology, Amrita University at Amritapuri, Kollam, Kerala, India. jjperry@scripps.edu

Methods (San Diego, Calif.)
|February 5, 2013
PubMed
Summary
This summary is machine-generated.

Small angle X-ray scattering (SAXS) offers detailed biophysical insights into protein interactions and conformational states. This technique, combined with other methods, enhances structural characterization and screening for systems biology research.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Small angle X-ray scattering (SAXS) is increasingly utilized for studying macromolecular behavior in solution.
  • SAXS provides crucial biophysical quantification of protein samples, including folding state, aggregation, and oligomerization.

Purpose of the Study:

  • To highlight the utility of SAXS in characterizing protein interactions, complex formation, and conformational dynamics.
  • To demonstrate how SAXS data, alone or integrated with other structural methods, can yield detailed structural information.

Main Methods:

  • Utilizing SAXS for initial sample quality assessment (aggregation, folding, dimensions).
  • Employing ab initio SAXS approaches and integrating data with crystallography/NMR for enhanced structural modeling.
  • Leveraging high-throughput SAXS in a 96-well plate format for screening diverse sample conditions and interactions.

Main Results:

  • SAXS enables detailed structural characterization, including domain organization and conformational states not resolved by other methods.
  • High-throughput SAXS facilitates screening for co-factors, inhibitors, and optimal conditions for crystallization.
  • SAXS can elucidate the impact of polymorphisms on protein assembly and activity, contributing to systems biology and comparative genomics.

Conclusions:

  • SAXS is a versatile tool for biophysical analysis of protein and macromolecular interactions.
  • Combining SAXS with crystallography, NMR, and computation offers a powerful, comprehensive approach to structural biology.
  • SAXS is essential for understanding complex biological systems, from molecular assembly to genomic variations.