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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: Jul 20, 2026

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Improved diffraction of antithrombin crystals grown in microgravity.

M R Wardell1, R Skinner, D C Carter

  • 1Department of Biochemistry and Molecular Biophysics, Washington University in St Louis, MO 63110-1093, USA. mrw@patmos.wustl.edu

Acta Crystallographica. Section D, Biological Crystallography
|September 7, 2001
PubMed
Summary

Crystals of antithrombin grew better in microgravity. Microgravity conditions improved crystal diffraction, enabling higher resolution for structural studies.

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Area of Science:

  • Biophysics
  • Crystallography
  • Space Science

Background:

  • Crystallization is crucial for determining protein structures.
  • Antithrombin is a vital protein for blood regulation.
  • Previous studies have explored microgravity's effect on crystal growth with variable results.

Purpose of the Study:

  • To compare the quality and diffraction properties of antithrombin crystals grown on Earth versus in microgravity.
  • To evaluate the effectiveness of a novel method for assessing crystal resolution from single diffraction images.

Main Methods:

  • Growing antithrombin crystals under terrestrial and microgravity (US Space Shuttle Flight STS-67) conditions.
  • Assessing crystal quality and indexing.
  • Utilizing a new procedure to estimate Bragg scatter resolution from single diffraction images.

Main Results:

  • Crystal quality was variable in both environments.
  • Microgravity-grown crystals generally diffracted better than Earth-grown crystals.
  • The best microgravity crystal diffracted to 2.6 angstroms, compared to 3 angstroms for the best Earth-grown crystal.

Conclusions:

  • Microgravity conditions appear to promote more ordered crystal growth for antithrombin.
  • The novel resolution estimation method is effective for evaluating crystal diffraction.
  • Further research may explore other factors influencing crystal quality in microgravity.