Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C.
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.
Sussman
J L
JL
Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Harel
M
M
Frolow
F
F
Varon
L
L
Toker
L
L
Futerman
A H
AH
Silman
I
I
D000110:Acetylcholinesterase / Q000302:isolation & purification*; D000818:Animals; D002846:Chromatography, Affinity; D003460:Crystallization; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D014101:Torpedo / Q000378:metabolism*; D014961:X-Ray Diffraction
D000110:Acetylcholinesterase; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase