The advances in recombinant DNA technology in recent years have had a
dramatic effect on the area of protein crystallization. Large amounts
of pure protem produced in various expression systems have made it pos
sible to conduct experiments that would have been impossible with mate
rial from natural sources. With many more laboratories becoming involv
ed in crystallizing proteins a great deal of new information has been
generated on techniques to eliminate the so called 'bottleneck of crys
tallization' in determining a three-dimensional protein structure. Mor
e and more new and interesting proteins are being submitted to this la
boratory for crystallization. Certain criteria may be set before cryst
allization trials are started, such as solubility, purity and aggregat
ion tendencies. The introduction of robots now facilitates the screeni
ng of crystallization conditions. In cases where no crystals have been
obtained after initial screening it can now be decided which possible
modifications can be made to the protein itself to improve the chance
s of obtaining crystals.