Crystallization and preliminary X-ray diffraction analysis of 11 S acetylcholinesterase.
The 11 S form of acetylcholinesterase from Electrophorus electricus was purified by affinity chromatography. The protein was crystallized from polyethylene glycol solutions. One crystal form proved suitable for x-ray diffraction studies. Preliminary x-ray analysis demonstrates that the space group of this crystal is F222. The unit cell dimensions are a = 141.0 +/- 0.2, b = 202.4 +/- 0.2, and c = 237.4 +/- 0.1 A. The diffraction is anisotropic, extending to at least 3.5 A along the a* and b* axes, but becoming weak beyond about 6 A along the c* axis. Crystal density measurements suggest that one complete 11 S tetramer occupies the asymmetric unit of the crystal.
Schrag
J D
JD
Department of Biochemistry, University of Arizona, Tucson 85721.
Schmid
M F
MF
Morgan
D G
DG
Phillips
G N
GN
Chiu
W
W
Tang
L
L
D000110:Acetylcholinesterase; D000818:Animals; D003460:Crystallization; D004593:Electrophorus / Q000378:metabolism*; D046911:Macromolecular Substances; D008970:Molecular Weight; D011092:Polyethylene Glycols; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011092:Polyethylene Glycols; D000110:Acetylcholinesterase