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Related Experiment Videos

Protein crystal perfection and its application.

John R Helliwell1

  • 1Department of Chemistry, University of Manchester, M13 9PL, England.

Acta Crystallographica. Section D, Biological Crystallography
|June 3, 2005
PubMed
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This review covers protein crystal perfection, detailing X-ray diffraction methods for assessment and applications in crystallography. It highlights techniques for analyzing crystal quality and discusses cryo- and room-temperature crystallography.

Area of Science:

  • Structural biology
  • Crystallography

Background:

  • Understanding protein crystal perfection is crucial for accurate structural determination.
  • X-ray diffraction is a primary technique in protein crystallography.

Purpose of the Study:

  • To review theoretical and practical knowledge of protein crystal perfection.
  • To describe X-ray methods for assessing crystal perfection and their applications.

Main Methods:

  • Review of X-ray diffraction physics applied to protein crystals.
  • Description of assessment techniques: mosaicity, topography, reciprocal-space mapping.
  • Discussion of Laue geometry and large-angle oscillation techniques.

Main Results:

  • Detailed explanation of X-ray diffraction methods for evaluating protein crystal quality.

Related Experiment Videos

  • Coverage of applications in various crystallographic geometries and temperature conditions.
  • Highlighting practical experience with freezing large crystals for neutron crystallography.

    • Conclusions:

    • Comprehensive overview of protein crystal perfection assessment and X-ray diffraction applications.
    • Emphasis on the importance of crystal quality for successful structural studies.
    • Practical insights into handling large crystals for advanced crystallographic techniques.