title: Crystallization of the Euplotes raikovi mating pheromone Er-1.
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.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
authors.forename: D
authors.initials: D
authors.lastname: Anderson
authors.forename: S
authors.initials: S
authors.lastname: Raffioni
authors.forename: P
authors.initials: P
authors.lastname: Luporini
authors.forename: R A
authors.initials: RA
authors.lastname: Bradshaw
authors.forename: D
authors.initials: D
authors.lastname: Eisenberg
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016798:Ciliophora / Q000502:physiology*; D003460:Crystallization; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification*; D010675:Pheromones / Q000302:isolation & purification*; D011487:Protein Conformation; D015800:Protozoan Proteins; D014961:X-Ray Diffraction
chemical_list: D008565:Membrane Proteins; D010455:Peptides; D010675:Pheromones; D015800:Protozoan Proteins; C057783:mating pheromone Er-1, Euplotes raikovi