Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination.
Counterdiffusion crystallization in capillary is a very simple, cost-effective, and practical procedure for obtaining protein crystals suitable for X-ray data analysis. Its principles have been derived using well-known concepts coupling the ideas of precipitation and diffusion mass transport in a restricted geometry. The counterdiffusion process has been used to simultaneously screen for optimal conditions for protein crystal growth, incorporate strong anomalous scattering atoms, and mix in cryogenic solutions in a single capillary tube. The crystals obtained in the capillary have been used in situ for X-ray analysis. The implementation of this technique linked to the advancement of current crystallography software leads to a powerful structure determination method consolidating crystal growth, X-ray data collection, and ab initio phase determination into one without crystal manipulation. We review the historical progress of counterdiffusion crystallization, its application to X-ray crystallography, and ongoing tool development for high-throughput protein structure determination.
Ng
Joseph D
JD
Department of Biological Sciences and the Laboratory for Structural Biology, University of Alabama at Huntsville, Huntsville, AL 35899, USA. ngj@email.uah.edu <ngj@email.uah.edu>
Gavira
José A
JA
García-Ruíz
Juan M
JM
D003460:Crystallization / Q000295:instrumentation / Q000379:methods*; D018360:Crystallography, X-Ray; D004058:Diffusion; D011506:Proteins / Q000737:chemistry*
D011506:Proteins