Time-Resolved X-ray Crystal Structure Analysis of Proteins

Abstract

With the use of extremely intense synchrotron radiation sources it has become possible to collect good quality x-ray diffraction data for protein crystals on a subsecond time-scale. This has led to the development of time-resolved protein crystallography, where the main objective is to determine the structures of short-lived intermediates during enzymatic reactions by monitoring the time dependence of the x-ray intensities. Furthermore, utilization of single-bunch mode in the 3rd generation synchrotron source enables us to shorten the time scale of the time-resolved protein crystallography to nano-or picosecond order. Possibility of nano-or picosecond protein crystallography in Accumlation Ring (KEK) and SPring-8 is disscussed.