LAUE DIFFRACTION PROTEIN CRYSTALLOGRAPHY AT THE NATIONAL SYNCHROTRON LIGHT-SOURCE

A new facility for the study of protein crystal structure using Laue d iffraction has been established at the X26 beam line of the National S ynchrotron Light Source (NSLS) at Brookhaven National Laboratory. The characteristics of the beam line and diffraction apparatus are describ ed. Selected results of some of the initial experiments are discussed briefly by beam line users to illustrate the scope of the experimental program. Because the Laue method permits the recording of large data sets in a single shot, one goal in establishing this facility has been to develop the means to study time-resolved structures within protein crystals. Systems being studied include: the reactions catalyzed by t rypsin; photolysis of carbonmonoxy myoglobin; and the photocycle of ph otoactive yellow protein.