The available methods are: annealing, dehydration, soaking and cross-linking.
The following publication is a review article that covers all methods used in this regard.
Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1173-80. Epub 2005 Aug 16.
Post-crystallization treatments for improving diffraction quality of protein crystals.
Heras B1, Martin JL.
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Abstract
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.
Cross-linked protein crystal technology, as either a protein stabilisation or enzyme immobilisation method, has garnered more attention recently. This method not only can retain the original activity of the protein molecule but can also significantly enhance the crystals' mechanical and chemical stability.
Please use the following link to view graphical illustration of how cross-linking cross- using glutaraldehyde stabilizes crystals: