| Literature DB >> 2850366 |
J L Sussman1, M Harel, F Frolow, L Varon, L Toker, A H Futerman, I Silman.
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.Entities:
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Year: 1988 PMID: 2850366 DOI: 10.1016/0022-2836(88)90213-6
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469