Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C

J L Sussman; M Harel; F Frolow; L Varon; L Toker; A H Futerman; I Silman

doi:10.1016/0022-2836(88)90213-6

Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C

J Mol Biol. 1988 Oct 5;203(3):821-3. doi: 10.1016/0022-2836(88)90213-6.

Authors

J L Sussman¹, M Harel, F Frolow, L Varon, L Toker, A H Futerman, I Silman

Affiliation

¹ Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.

PMID: 2850366
DOI: 10.1016/0022-2836(88)90213-6

Abstract

A dimeric form of acetylcholinesterase from Torpedo californica was purified to homogeneity by affinity chromatography subsequent to solubilization with a phosphatidylinositol-specific phospholipase C of bacterial origin. Bipyramidal crystals of the enzyme were obtained from solutions in polyethylene glycol 200. The crystals diffract to 2.0 A (1 A = 0.1 nm) resolution. They were found to be orthorhombic, space group P2221, with a = 163.4(+/- 0.2) A, b = 112.1(+/- 0.2) A, c = 81.3(+/- 0.1) A.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Acetylcholinesterase / isolation & purification*
Animals
Chromatography, Affinity
Crystallization
Phosphatidylinositol Diacylglycerol-Lyase
Phosphoinositide Phospholipase C
Phosphoric Diester Hydrolases / metabolism*
Torpedo / metabolism*
X-Ray Diffraction

Substances

Acetylcholinesterase
Phosphoric Diester Hydrolases
Phosphoinositide Phospholipase C
Phosphatidylinositol Diacylglycerol-Lyase