Laue diffraction as a tool in dynamic studies: Hydrolysis of a transiently stable intermediate in catalysis by trypsin
- Brookhaven National Lab., Upton, NY (United States)
- State Univ. of New York, Brooklyn, NY (United States). Dept. of Biochemistry
- Brandeis Univ., Waltham, MA (United States). Rosenstiel Basic Medical Science Center
- Center for Advanced Biotechnology and Medicine, Piscataway, NJ (United States)
- Univ. of Tromso (Norway). Inst. of Mathematics and Physical Science
A transiently stable intermediate in trypsin catalysis, guanidinobenzyol-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.
- Research Organization:
- Brookhaven National Lab., Upton, NY (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States); National Science Foundation, Washington, DC (United States)
- DOE Contract Number:
- AC02-76CH00016
- OSTI ID:
- 10105332
- Report Number(s):
- BNL-48058; CONF-9201120-1; ON: DE93003141
- Resource Relation:
- Conference: Royal Society discussion meeting on time resolved macromolecular crystallography,London (United Kingdom),29-30 Jan 1992; Other Information: PBD: [1992]
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
36 MATERIALS SCIENCE
TRYPSIN
CRYSTALLOGRAPHY
CATALYSIS
CRYSTAL STRUCTURE
X-RAY DIFFRACTION
HYDROLYSIS
ENZYMES
400201
665100
360606
CHEMICAL AND PHYSICOCHEMICAL PROPERTIES
NUCLEAR TECHNIQUES IN CONDENSED MATTER PHYSICS
PHYSICAL PROPERTIES