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Related Concept Videos

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...
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 6, 2026

Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin
06:29

Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin

Published on: March 3, 2021

Strategies for processing diffraction data from randomly oriented particles.

Veit Elser1

  • 1Department of Physics, Cornell University Ithaca, NY 14853-2501, USA. ve10@cornell.edu

Ultramicroscopy
|November 25, 2010
PubMed
Summary
This summary is machine-generated.

Serial single-shot X-ray diffraction offers superior information content for determining virus and protein structures compared to particle ensemble methods. This approach, while challenging, is essential for accurate 3D structure determination.

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Last Updated: Jun 6, 2026

Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin
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Published on: March 3, 2021

Synthesis and Microdiffraction at Extreme Pressures and Temperatures
07:26

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Published on: October 7, 2013

Microcrystallography of Protein Crystals and In Cellulo Diffraction
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Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Area of Science:

  • Structural biology
  • Biophysics
  • X-ray crystallography

Background:

  • High-intensity free-electron X-ray sources offer potential for non-crystalline structure determination.
  • Current methods include serial single-shot data collection and averaged cross-correlation data from particle ensembles.

Purpose of the Study:

  • To compare the information content of two proposed non-crystalline diffraction data collection schemes.
  • To evaluate their suitability for virus and protein structure determination.

Main Methods:

  • Comparative analysis of information content between serial single-shot and cross-correlation data collection schemes.
  • Constraint counting arguments to assess data deficiency for 3D structure determination.

Main Results:

  • The serial single-shot approach provides superior information content for structure determination.
  • The cross-correlation scheme exhibits data deficiency, particularly for 3D structure determination.

Conclusions:

  • Serial single-shot data collection is the preferred method for non-crystalline structure determination due to higher information content.
  • The cross-correlation method is limited by data deficiency for complex structural analyses.