Abstract
Protein crystallography is one of the most powerful methods in structural biology to determine the three-dimensional structures of protein molecules at an atomic resolution. However, it is often difficult and laborious to obtain a welldiffracting crystal suitable for structure determination. Since the gravity is one of factors affecting protein crystallization, the microgravity environment has been used to improve the quality of protein crystals. On the other hand, development of the advanced synchrotron facilities such as SPring-8 enabled us to utilize very strong X-ray beams that have almost ideal character for the use in protein crystallography. Here we describe the recent progress of the synchrotron techniques in protein crystallography and discuss the effective crystallization under microgravity for synchrotron experiments.
