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.
Recenzijas
This volume provides a methodological overview that would be difficult to find elsewhere...[ ..] it is an excellent, up-to-date review of the methods currently used by x-ray crystallography laboratories around the world. As such it will certainly be a useful reference for laboratories taking advantage of x-ray crystallography as a research tool. The Quarterly Review of Biology
D.W.J. Cruickshank: Time-resolved macromolecular crystallography:
introductory remarks and a little history; Keith Moffat, Ying Chen, Kingman
Ng, Duncan McRee & Elizabeth D. Getzoff: Time-resolved crystallography:
principles, problems and practice; Gian Luigi Rossi, Andrea Mozzarelli,
Alessio Peracchi & Claudio Rivetti: Time course of chemical and structural
events in protein crystals measured by microspectrophotometry; Hans D.
Bartunik, Lesley J. Bartunik & Hans Viehmann: Time-resolved X-ray diffraction
studies of enzymes under cryoconditions; J.R. Helliwell: Synchrotron X-ray
crystallography techniques: time-resolved aspects of data collection; J.E.T.
Corrie, Y. Katayama, G.P. Reid, M. Anson & D.R. Trentham: The development and
application of photosensitive caged compounds to aid time-resolved structure
determination of macromolecules; E.M.H. Duke, A. Hadfield, S. Walters, S.
Wakatsuki, R.K. Bryan & L.N. Johnson: Time-resolved diffraction studies on
glycogen phosphorylase b; Inger Anderson, Ian J. Clifton, Steven L. Edwards,
Vilmos Fulop, Andrea T. Hadfield, Janos Hadju, Par Nordlund, Paul
Phizackerley, Michael Soltis, Soichi Wakatsuki: On the scope and limitations
of the Laue method in kinetic crystallography: studies with macromolecules;
Axel Scheidig, Emil F. Pai, I. Schlichting, John Corrie, Gordon P. Reid,
Alfred Wittinghofer & Roger S. Goody: Time-resolved crystallography on H-ras
p21; Dagmar Ringe, Barry L. Stoddard, John Bruhnke, Paula Koenigs & Ned
Porter: Can Laue catch Maxwell?: observation of short-lived species by Laue
X-ray crystallography; Paul T. Singer, Robert P. Carty, Lonny E. Berman, Ilme
Schlichting, Ann Stock, Arne Smalas, Zhouping Cai, Walter F. Mangel, Keith W.
Jones & Robert M. Sweet: Laue diffraction as a tool in dynamic studies:
hydrolysis of a transiently stable intermediate in catalysis by trypsin; A.
Liljas, M. Carlsson, K. Hakansson, M. Lindahl, L.A. Svensson & A. Wehnert:
Laue and monochromatic crystallography on carbonic anhydrase; D.M. Blow, P.
Brick, C.A. Collyer, J.D. Goldberg & O. Smart: Conventional X-ray diffraction
approaches to the study of enzyme mechanism: serine proteinases,
aminoacyl-tRNA synthetases and xylose isomerase; Gregory A. Petsko: Art is
long and time is fleeting: the current problems and future prospects for
time-resolved enzyme crystallography.
