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« Previous AbstractMolecular analysis of the pheromone and pheromone receptor genes of Ustilago hordei    Next AbstractA challenging case for protein crystal structure determination: the mating pheromone Er-1 from Euplotes raikovi »

J Mol Biol


Title:Crystallization of the Euplotes raikovi mating pheromone Er-1
Author(s):Anderson D; Raffioni S; Luporini P; Bradshaw RA; Eisenberg D;
Address:"Department of Chemistry and Biochemistry, University of California, Los Angeles 90024"
Journal Title:J Mol Biol
Year:1990
Volume:216
Issue:1
Page Number:1 - 2
DOI: 10.1016/S0022-2836(05)80055-5
ISSN/ISBN:0022-2836 (Print) 0022-2836 (Linking)
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"
Keywords: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;
Notes:"MedlineAnderson, D Raffioni, S Luporini, P Bradshaw, R A Eisenberg, D eng DK32465/DK/NIDDK NIH HHS/ GM31299/GM/NIGMS NIH HHS/ GM39558/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. Netherlands 1990/11/05 J Mol Biol. 1990 Nov 5; 216(1):1-2. doi: 10.1016/S0022-2836(05)80055-5"

 
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