Publisher's Synopsis
X-ray diffraction studies have made outstanding contributions to structural molecular biology. The advent of high-intensity synchrotron radiation sources, coupled with the revival of the Laue method, has now made possible the rapid collection of X-ray crystallography data. As a result, protein and virus crystallography is now progressing from studies of equilibrium structures to time-resolved studies of structures at reaction stages. The full exploitation of the synchrotron Laue method for the study of dynamic events in crystals requires many developments in physics, chemistry, and biochemistry: the papers presented in this volume aim to report some of the striking results that have already been obtained and to discuss and identify necessary future developments.
