Title : Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C - Sussman_1988_J.Mol.Biol_203_821 |
Author(s) : Sussman JL , Harel M , Frolow F , Varon L , Toker L , Futerman AH , Silman I |
Ref : Journal of Molecular Biology , 203 :821 , 1988 |
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. |
PubMedSearch : Sussman_1988_J.Mol.Biol_203_821 |
PubMedID: 2850366 |
Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I (1988)
Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C
Journal of Molecular Biology
203 :821
Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I (1988)
Journal of Molecular Biology
203 :821