Accession Number : ADA268487


Title :   The Crystallization of Acetylcholinesterase (AChE) from Torpedo Electric Organ


Descriptive Note : Annual rept. 15 Jan 87-14 Jan 89 (Final),


Corporate Author : WEIZMANN INST OF SCIENCE REHOVOT (ISRAEL) DEPT OF NEUROBIOLOGY


Personal Author(s) : Silman, I ; Sussman, J L


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a268487.pdf


Report Date : 18 Jul 1991


Pagination or Media Count : 25


Abstract : The objective of this project is the crystallization of the enzyme acetylcholinesterase (AChE), with the long-term objective of determining its three-dimensional structure and, thereby, the detailed topography of its active site. Torpedo electric organ was selected since it is a rich source of AChE and possesses an amino acid sequence very similar to that of mammalian AChE. A dimeric form of this enzyme was purified by a procedure which involved selective solubilization with a phosphatidylinositol-specific phospholipase C of bacterial origin, followed by affinity chromatography employing a Sepharose conjugate of a suitable quaternary affinity ligand. A highly purified AChE preparation was obtained in amounts which permitted a systematic attempt to crystallize the enzyme. In order to obtain a crystal form of the ACHE preparation suitable for high-resolution X-ray studies, we examined hundreds of different crystallization conditions. As a result we were able to obtain three (3) different crystal forms which diffract to better than 3 A resolution.... RAV, Acetylcholinesterase, X- Ray Crystallography, Torpedo californica, Crystallization, Three-dimensional structure, Enzymes, Acetylcholine.


Descriptors :   *ENZYMES , *CRYSTALLIZATION , *ACETYLCHOLINESTERASE , X RAY DIFFRACTION , HIGH RESOLUTION , X RAYS , CRYSTALLOGRAPHY , CHROMATOGRAPHY , ACETYLCHOLINE , DIMERS , AMINO ACIDS , TOPOGRAPHY , SEQUENCES , THREE DIMENSIONAL , LIGANDS


Subject Categories : Biochemistry


Distribution Statement : APPROVED FOR PUBLIC RELEASE