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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...
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...

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Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
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Methods and software for diffuse X-ray scattering from protein crystals.

Michael E Wall1

  • 1Center for Nonlinear Studies, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. mewall@lanl.gov

Methods in Molecular Biology (Clifton, N.J.)
|June 3, 2009
PubMed
Summary
This summary is machine-generated.

Researchers mapped protein conformational distributions using diffuse X-ray scattering. This technique offers insights into protein dynamics, with new software available for broader scientific use.

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Area of Science:

  • Structural Biology
  • Biophysics
  • X-ray Crystallography

Background:

  • Proteins exist in dynamic conformational distributions, not static structures.
  • Experimental methods to fully characterize these distributions are limited.
  • Diffuse X-ray scattering is a promising technique for probing protein dynamics.

Purpose of the Study:

  • To develop and apply diffuse X-ray scattering for characterizing protein conformational distributions.
  • To generate the first 3D reciprocal-space maps of diffuse X-ray reflections from protein crystals.
  • To make the analysis software publicly available for the scientific community.

Main Methods:

  • Measurement of 3D reciprocal-space maps of diffuse X-ray reflection intensity from protein crystals.
  • Analysis of diffuse scattering data to characterize protein conformational distributions.
  • Development and release of the Lunus software package for data analysis.

Main Results:

  • Successfully generated the first 3D reciprocal-space maps of diffuse X-ray reflections from protein crystals.
  • Demonstrated the utility of diffuse X-ray scattering in characterizing protein conformational distributions.
  • Validated the Lunus software for analyzing diffuse scattering data.

Conclusions:

  • Diffuse X-ray scattering is a powerful method for studying protein conformational dynamics.
  • X-ray beamlines can be adapted for diffuse scattering measurements on protein crystals.
  • The publicly available Lunus software will facilitate future research in this area.