Work

Crystallization and preliminary X-ray diffraction analysis of 11 S acetylcholinesterase.

Year: 1988

Type: article

Abstract: 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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)81588-0

Authors: J D Schrag, M F Schmid, D G Morgan, G N Phillips, W Chiu, L Tang

Institution: University of Arizona

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institutes of Health, National Center for Research Resources