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Detecting and overcoming crystal twinning

T O Yeates1

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.

Methods in Enzymology
|January 1, 1997
PubMed
Summary
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Merohedral twinning in protein crystals is common and can affect diffraction data. Routine intensity statistics tests are recommended to identify both partial and perfect twinning in relevant space groups.

Area of Science:

  • Crystallography
  • Structural Biology
  • Biophysics

Background:

  • Twinning is a frequent phenomenon in protein crystal diffraction.
  • Merohedral twinning, a specific type, can obscure true crystallographic intensities in diffraction patterns.
  • Distinguishing between partial and perfect twinning is crucial for accurate data interpretation.

Purpose of the Study:

  • To highlight the prevalence and impact of merohedral twinning in protein crystallography.
  • To emphasize the importance of identifying merohedral twinning for reliable structural analysis.
  • To advocate for routine application of statistical tests for twinning detection.

Main Methods:

  • Analysis of crystallographic intensity statistics.
  • Examination of diffraction patterns for twinning indicators.

Related Experiment Videos

  • Statistical tests designed to differentiate between twinned and untwinned data.

    • Main Results:

    • Merohedral twinning is common in protein crystals.
    • Diffraction patterns from merohedral twins do not directly represent individual crystallographic intensities.
    • Partial (twin fraction < 1/2) and perfect (twin fraction = 1/2) twinning are identifiable through intensity statistics.

    Conclusions:

    • Routine application of intensity statistics tests is essential for space groups susceptible to merohedral twinning.
    • Failure to identify merohedral twinning can lead to inaccurate structural data.
    • Implementing these tests ensures the integrity of crystallographic data derived from protein crystals.