Purification, crystallization, and preliminary X-ray data for porcine fumarase. Academic Article

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.

authors

• Sacchettini, James

published proceedings

• J Biol Chem

author list (cited authors)

• Sacchettini, J. C., Meininger, T., Roderick, S., & Banaszak, L. J.

citation count

• 20

complete list of authors

• Sacchettini, JC||Meininger, T||Roderick, S||Banaszak, LJ

publication date

• November 1986

publisher

• Elsevier  Publisher

published in

• Journal of Biological Chemistry  Journal

keywords

• Animals
• Crystallization
• Fumarate Hydratase
• Myocardium
• Protein Conformation
• Swine
• X-Ray Diffraction

PubMed Central ID

• 3771571

Digital Object Identifier (DOI)

• 10.1016/s0021-9258(18)66850-4

start page

• 15183

end page

• 15185

volume

• 261

issue

• 32

URL

• http://dx.doi.org/10.1016/s0021-9258(18)66850-4