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Time-Resolved X-Ray Diffraction Studies of Enzymes under Cryoconditions [and Discussion]
Hans D. Bartunik, Lesley J. Bartunik, Hans Viehmann, J. Hajdu and G. A. Petsko
Philosophical Transactions: Physical Sciences and Engineering
Vol. 340, No. 1657, Time-Resolved Macromolecular Crystallography (Aug. 15, 1992), pp. 209-220
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/53888
Page Count: 12
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Cryoenzymological techniques provide a means of initiating enzymatic reactions in crystals homogeneously and of prolonging the lifetimes of intermediate reaction steps. Catalytic intermediates may accumulate to sufficiently high population for X-ray crystal structure analysis by time-resolved monochromatic or Laue diffraction data collection using synchrotron radiation. Due to short exposure times, intermediates may be studied at moderately low temperatures. A combination of cryoenzymology and time-resolved crystallography has been applied to crystal structure analysis at high resolution of an acyl-enzyme intermediate of a productive reaction catalysed by porcine pancreatic elastase.
Philosophical Transactions: Physical Sciences and Engineering © 1992 Royal Society