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

作者信息

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

机构信息

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

出版信息

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

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.