2007 Volume 34 Issue 3 Pages 131-138
Structural Biology provides vital information for understanding functions of molecular machineries of life. X-ray protein crystallography has been and will be a primary method of choice for elucidating atomic details of macromolecular complexes. Crystallization of proteins and their complexes remains one of the bottlenecks in structural studies and of date there are numerous groups around the globe who are developing new methods for crystallization and evaluation of protein crystals. This review starts with a short introduction on the principles of protein crystallization, followed by a description of recent developments for automation of protein crystallization, detection and evaluation by visible and UV light. We then discuss methodology to evaluate crystal quality by X-ray beams and ways to facilitate data collection from micro-crystal on synchrotron beam lines.