X-ray crystallography is the most powerful method for determining the three-dimensional structure of biological macromolecules. One of the major obstacles in the process is the production of high-quality crystals for structure determination. All too often, crystals are produced that are of poor quality and are unsuitable for diffraction studies. This review provides a compilation of post-crystallization methods that can convert poorly diffracting crystals into data-quality crystals. Protocols for annealing, dehydration, soaking and cross-linking are outlined and examples of some spectacular changes in crystal quality are provided. The protocols are easily incorporated into the structure-determination pipeline and a practical guide is provided that shows how and when to use the different post-crystallization treatments for improving crystal quality. © 2005 International Union of Crystallography - all rights reserved.
CITATION STYLE
Heras, B., & Martin, J. L. (2005, September). Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallographica Section D: Biological Crystallography. https://doi.org/10.1107/S0907444905019451
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