Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius)

J Mol Biol. 1988 Jul 20;202(2):349-53. doi: 10.1016/0022-2836(88)90464-0.

Abstract

The crystal and molecular structure of the minor component of pike parvalbumins has been determined at 1.93 A resolution by molecular replacement (1 A = 0.1 nm). The crystals are orthorhombic, space group P2(1)2(1)2 with a = 59.62 A, b = 59.83 A and c = 26.35 A. A location of the secondary cation binding site is proposed for this parvalbumin of the beta phylogenetic series.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Crystallography
  • Muscle Proteins*
  • Parvalbumins*
  • Salmonidae

Substances

  • Muscle Proteins
  • Parvalbumins