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Journal Article

Laue diffraction as a tool in dynamic studies: hydrolysis of a transiently stable intermediate in catalysis by trypsin

MPS-Authors
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Schlichting,  Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://rsta.royalsocietypublishing.org/content/340/1657/285.full.pdf
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https://doi.org/10.1098/rsta.1992.0067
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Citation

Singer, P. T., Carty, R. P., Berman, L. E., Schlichting, I., Stock, A., Smalas, A., et al. (1992). Laue diffraction as a tool in dynamic studies: hydrolysis of a transiently stable intermediate in catalysis by trypsin. Philosophical Transactions of the Royal Society of London A, 340(1657), 285-300. doi:10.1098/rsta.1992.0067.


Cite as: https://hdl.handle.net/21.11116/0000-0000-6015-C
Abstract
A transiently stable intermediate in trypsin catalysis, guanidinobenzoyl-Ser-195 trypsin, can be trapped and then released by control of the pH in crystals of the enzyme. This effect has been investigated by static and dynamic white-beam Laue crystallography. Comparison of structures determined before and immediately after a pH jump reveals the nature of concerted changes that accompany activation of the enzyme. Careful analysis of the results of several structure determinations gives information about the reliability of Laue results in general. A study of multiple exposures taken under differing conditions of beam intensity, crystal quality, and temperature revealed information about ways to control damage of specimens by the X-ray beam.