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Protein crystals and their evil twins.
1UCLA Department of Chemistry and Biochemistry, DOE Laboratory of Structural Biology and Molecular Medicine, 405 Hilgard Avenue, Box 951569, Los Angeles CA 90095-1569, USA. yeates@mbi.ucla.edu
Structure (London, England : 1993)
|June 16, 1999
Summary
Crystal twinning, a common issue in protein diffraction, can be detected using various methods. Researchers emphasize routine checks to identify and address twinning in crystallographic data.
Area of Science:
- Crystallography
- Structural Biology
- Biophysics
Background:
- Crystal twinning is a crystallographic phenomenon where two or more related crystal lattices grow together.
- It can significantly complicate the interpretation of diffraction data, leading to inaccurate structural models.
- Understanding and identifying twinning is crucial for successful protein structure determination.
Purpose of the Study:
- To review different types of crystal twinning.
- To highlight methods for detecting twinning in protein diffraction data.
- To emphasize the importance of routine checks for twinning.
Main Methods:
- Review of recent scientific literature on crystal twinning.
- Survey of crystallographic databases to assess the prevalence and detection of twinning.
- Discussion of established and emerging techniques for identifying twinned crystals.
Main Results:
- Various types of crystal twinning exist and are well-documented.
- Several methods are available for detecting twinning from diffraction data.
- A significant number of studies may be affected by undetected twinning.
Conclusions:
- Routine checks for crystal twinning should be an integral part of the crystallographic workflow.
- Awareness and application of detection methods can improve data quality and structural model reliability.
- Further development of automated detection methods could benefit the field.