Post-crystallization treatments for improving diffraction quality of protein crystals.
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.
Heras
Begoña
B
Institute for Molecular Bioscience and ARC Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane QLD 4072, Australia. b.heras@imb.uq.edu.au
Martin
Jennifer L
JL
D003432:Cross-Linking Reagents; D015925:Cryopreservation; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods* / Q000592:standards; D014867:Water / Q000737:chemistry
D003432:Cross-Linking Reagents; D014867:Water