Low-temperature and time-resolved protein crystallography using synchrotron radiation

Abstract

Internal motions in protein molecules may be investigated by stationary and time-resolved crystallography using synchrotron radiation and crystal cooling to low temperatures. The experimental techniques involved in such studies, and first results of applications to structure determination to high resolution at temperatures down to 100 K, and to time-resolved data collection on a submillisecond time scale for carbonmonoxy myoglobin following laser photolysis of the ligand, are described.