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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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Related Experiment Video

Updated: Jun 3, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

The design of macromolecular crystallography diffraction experiments.

Gwyndaf Evans1, Danny Axford, Robin L Owen

  • 1Diamond Light Source, Harwell Science and Innovation Campus, Didcot, England. gwyndaf.evans@diamond.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|April 5, 2011
PubMed
Summary

This study details optimizing X-ray diffraction measurements for macromolecular crystallography. It guides users on maximizing data quality by integrating sample preparation with beamline operations for accurate structure determination.

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Last Updated: Jun 3, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Macromolecular structure determination relies on X-ray diffraction data.
  • Obtaining high-quality diffraction data requires optimized crystal samples and X-ray beamlines.

Purpose of the Study:

  • To describe the experimental design for fully exploiting both macromolecular samples and X-ray beamlines.
  • To guide synchrotron users in making informed decisions for optimal diffraction measurements.

Main Methods:

  • Integrating sample preparation strategies with beamline operational parameters.
  • Developing a systematic approach to data acquisition at synchrotron facilities.

Main Results:

  • Demonstration of experimental strategies that maximize diffraction data quality.
  • Identification of key user decisions impacting measurement outcomes.

Conclusions:

  • Optimizing the synergy between sample quality and beamline performance is crucial for successful macromolecular crystallography.
  • User awareness and informed decision-making are vital for efficient synchrotron data collection.