A pentameric form of human serum amyloid P component. Crystallization, X-ray diffraction and neutron scattering studies

J Mol Biol. 1988 Jul 5;202(1):169-73. doi: 10.1016/0022-2836(88)90529-3.

Abstract

Human serum amyloid P component crystallizes from sodium acetate buffer (pH 5.5) in the presence of calcium and polyethylene glycol 6000, at 4 degrees C. The space group is P2(1) and the cell parameters are a = 69.0 A (1 A = 0.1 nm), b = 99.3 A, c = 96.8 A, beta = 96.1. Density considerations supported by neutron scattering and gel filtration experiments indicate that the species crystallized is pentameric. The orientation of the pentamer 5-fold axis is determined and a crystal packing for the discs is proposed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Humans
  • Macromolecular Substances
  • Neutrons
  • Scattering, Radiation
  • Serum Amyloid P-Component*
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Serum Amyloid P-Component