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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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Related Experiment Video

Updated: May 17, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

The collection of high-resolution electron diffraction data.

Tamir Gonen1

  • 1Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 8, 2012
PubMed
Summary
This summary is machine-generated.

Electron crystallography is advancing membrane protein structure determination. This chapter details electron diffraction data collection protocols, crucial for improving this technique.

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
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Last Updated: May 17, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Area of Science:

  • Structural Biology
  • Biophysics

Background:

  • Electron crystallography has enabled atomic-resolution determination of membrane proteins.
  • Despite its potential, the technique is still developing in areas like 2D crystallization and data analysis.
  • Data collection is a key component of electron crystallography.

Purpose of the Study:

  • To provide detailed protocols for electron diffraction data collection in electron crystallography.
  • To address the current limitations in electron crystallography by focusing on data collection.

Main Methods:

  • Microscope setup for electron diffraction.
  • Electron diffraction data collection procedures.
  • Troubleshooting common issues during data collection.

Main Results:

  • Established protocols for effective electron diffraction data collection.
  • Guidelines for optimizing microscope settings.
  • Solutions for common problems encountered during data acquisition.

Conclusions:

  • Detailed protocols are essential for advancing electron crystallography.
  • Improved data collection methods will enhance membrane protein structure determination.
  • This chapter serves as a practical guide for researchers in the field.