Purification, crystallization, and preliminary X-ray data for porcine fumarase. | Academic Article individual record
abstract

Single crystals of fumarase purified from pig heart have been prepared from solutions containing polyethylene glycol. The crystals give diffraction data corresponding to Bragg spacings of 2.0 A and contain a single subunit of the enzyme in the asymmetric unit of the C222 unit cell. Therefore, the subunits of this tetrameric molecule are arranged with the point symmetry group 222. The present purification scheme and studies of the NH2-terminal amino acid sequences suggest that only a single form of the enzyme is present, and it is thought to be the mitochondrial enzyme.

author list (cited authors)
Sacchettini, J. C., Meininger, T., Roderick, S., & Banaszak, L. J.
publication date
1986
keywords
  • Fumarate Hydratase
  • X-Ray Diffraction
  • Crystallization
  • Myocardium
  • Protein Conformation
  • Swine
  • Animals
citation count

19