Crystallization of the Euplotes raikovi mating pheromone Er-1

J Mol Biol. 1990 Nov 5;216(1):1-2. doi: 10.1016/S0022-2836(05)80055-5.

Abstract

A protein mating pheromone Er-1 from the ciliate Euplotes raikovi has been crystallized from (NH4)2SO4 in two forms. Both are suitable for structural studies to at least 2.8 A resolution. Both unit cell sizes are consistent with a tetramer of molecular weight 17,640 in the asymmetric unit.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ciliophora / physiology*
  • Crystallization
  • Membrane Proteins*
  • Molecular Sequence Data
  • Peptides / isolation & purification*
  • Pheromones / isolation & purification*
  • Protein Conformation
  • Protozoan Proteins*
  • X-Ray Diffraction

Substances

  • Membrane Proteins
  • Peptides
  • Pheromones
  • Protozoan Proteins
  • mating pheromone Er-1, Euplotes raikovi