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 singlebunch mode at the third generation synchrotron sources enables us to shorten the time-scale of the time-resolved protein crystallography down to nanosecond order. Feasibility of singlepulse Laue diffraction experiment on protein crystals is discussed.
