FEASIBILITY AND REALIZATION OF SINGLE-PULSE LAUE DIFFRACTION ON MACROMOLECULAR CRYSTALS AT ESRF

Laue diffraction patterns with an exposure time of ca 60 ps have been acquired at the European Synchrotron Radiation Facility (ESRF) on prot ein crystals by using the single-bunch mode of the storage ring. A 10 ns laser pulse initiating photodissociation was synchronized with the X-ray pulse. The potential for a quantitative detection of conformatio nal changes in proteins on the nanosecond timescale with this techniqu e is demonstrated using the example of carbonmonoxymyoglobin, from sim ulations and real data. The instrumental aspects of the experiment (hi ghly intense X-ray beam, fast shutter system, Laue camera, detector, l aser apparatus and synchronization technique) are emphasized.