The papers presented in this volume report the striking progress X-ray diffraction has facilitated in the study of structural molecular biology. Coupled with the revival of the Laue method, the advent of high-intensity synchrotron radiation sources has made possible the rapid collection of X-ray crystallography data, thereby allowing protein and virus crystallography to progress from studies of equilibrium structures to time-resolved studies of structures at reaction stages. The book also details the many recent technological developments in physics, chemistry and biochemistry that have been critical for the full exploitation of the synchrotron Laue method in the study of dynamic events in crystals. Necessary future developments are discussed.

About the Author

D. W. J. Cruickshank is at UMIST, Manchester. J. R. Helliwell is at University of Manchester.

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