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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.
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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
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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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Updated: May 15, 2026

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
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Continuous X-ray diffractive field in protein nanocrystallography.

Ruben A Dilanian1, Victor A Streltsov, Harry M Quiney

  • 1ARC Centre of Excellence for Coherent X-ray Science, School of Physics, The University of Melbourne, Victoria, Australia. roubend@unimelb.edu.au

Acta Crystallographica. Section A, Foundations of Crystallography
|December 20, 2012
PubMed
Summary
This summary is machine-generated.

New X-ray laser methods enable protein structure determination from nanocrystals. This approach accounts for crystal imperfections, offering a unique crystallographic solution for challenging samples.

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Last Updated: May 15, 2026

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Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
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Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies

Published on: April 11, 2021

Area of Science:

  • Structural biology
  • Crystallography
  • Biophysics

Background:

  • X-ray free-electron laser (XFEL) sources advance protein nanocrystal analysis.
  • Small crystal size and structural imperfections create complex diffraction patterns.
  • Existing methods struggle with low-quality or imperfect protein crystals.

Purpose of the Study:

  • To develop novel protein structure determination methods for nanocrystalline samples.
  • To address challenges posed by crystal size and structural imperfections in diffraction data.
  • To enable protein structure analysis under near-native conditions.

Main Methods:

  • Utilizing advanced X-ray diffraction techniques with XFEL sources.
  • Developing data analysis algorithms to account for size and defect effects.
  • Implementing a unique crystallographic approach tailored for nanocrystals.

Main Results:

  • Demonstrated a viable method for structural analysis of protein nanocrystals.
  • Successfully modeled the impact of structural imperfections on diffraction patterns.
  • Provided a unique crystallographic solution for challenging protein samples.

Conclusions:

  • The developed approach offers a powerful tool for protein structure determination.
  • This method overcomes limitations of traditional crystallography for small and imperfect crystals.
  • Enables near-native protein structure analysis, advancing structural biology.