Laue diffraction as a tool in dynamic studies: hydrolysis of a transiently stable intermediate in catalysis by trypsin
- 15 August 1992
- journal article
- Published by The Royal Society in Philosophical Transactions A
- Vol. 340 (1657) , 285-300
- https://doi.org/10.1098/rsta.1992.0067
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.Keywords
This publication has 13 references indexed in Scilit:
- Optical design and performance of the X25 hybrid wiggler beam line at the National Synchrotron Light SourceReview of Scientific Instruments, 1992
- Experimental strategies in Laue crystallographyJournal of Applied Crystallography, 1991
- Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl)trypsinBiochemistry, 1990
- Progress with Laue diffraction studies on protein and virus crystalsBiochemistry, 1990
- The recording and analysis of synchrotron X-radiation Laue diffraction photographsJournal of Applied Crystallography, 1989
- Evaluation of single-crystal X-ray diffraction data from a position-sensitive detectorJournal of Applied Crystallography, 1988
- Preliminary study of a phase transformation in insulin crystals using synchrotron-radiation Laue diffractionActa crystallographica Section B, Structural science, crystal engineering and materials, 1988
- X-ray Laue diffraction from crystals of xylose isomerase.Proceedings of the National Academy of Sciences, 1988
- Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystalNature, 1987
- Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallographyJournal of Applied Crystallography, 1987