Accession Number : ADA306003
Title : X-Ray Crystallographic Studies on Acetylcholinesterase and on Its Interaction with Anticholinesterase Agents.
Descriptive Note : Midterm rept. 30 Apr 93-29 Apr 94,
Corporate Author : WEIZMANN INST OF SCIENCE REHOVOT (ISRAEL)
Personal Author(s) : Silman, Israel ; Sussman, Joel L.
PDF Url : ADA306003
Report Date : 24 NOV 1994
Pagination or Media Count : 45
Abstract : The EMBL-DESY synchrotron facility at Hamburg was employed to collect a complete 2.3 A data set for a crystal of native Torpedo AChE, as well as for complexes with reversible ligands, including edrophonium, d-tubocurarine and huperzine A, diffracting to similar resolution. The X26c Laue beam line at the NSLS synchrotron facility at Brookhaven National Laboratory (BNL) was used to obtain a Laue diffraction pattern for a crystal of native Torpedo AChE, diffracting out to 2.8 A. This is a first step towards our long-range objective of performing time-resolved X-ray crystallographic measurements on AChE. A complete 2.8 A data set was collected on a covalent adduct of Torpedo AChE with the transition-state analog, m -(N,N,N-trimethylammonio) trifluoroacetophenone, which serves as a powerful, quasi-irreversible inhibitor. This permitted detailed analysis of the multiple ligand-AChE interactions.
Descriptors : *X RAYS, *ACETYLCHOLINESTERASE, *CHOLINESTERASE INHIBITORS, *CRYSTALLOGRAPHY, DATA BASES, MEASUREMENT, TORPEDOES, FACILITIES, TIME, DIFFRACTION, REVERSIBLE, LIGANDS, PATTERNS, SYNCHROTRONS.
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE