Crystallization of the Euplotes raikovi mating pheromone Er-1.
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.
Anderson
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Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
Raffioni
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Luporini
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Bradshaw
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RA
Eisenberg
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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
D008565:Membrane Proteins; D010455:Peptides; D010675:Pheromones; D015800:Protozoan Proteins; C057783:mating pheromone Er-1, Euplotes raikovi