Crystallographic characterization and molecular symmetry of edestin, a legumin from hemp.
Edestin, a legumin class reserve protein from hemp seeds having six identical subunits was crystallized from ammonium phosphate at pH 5 and subsequently characterized by X-ray diffraction. The crystals are of space group R32 with a = 127 A and gamma = 116 degrees having an equivalent triply centered hexagonal cell of a = b = 215 A, c = 80 A. There is one hexameric protein in the rhombohedral unit cell, hence the subunits of the Edestin molecule must be arranged with 32 point group symmetry.
Patel
S
S
University of California, Department of Biochemistry, Riverside 92521.
Cudney
R
R
McPherson
A
A
D002188:Cannabis; D003460:Crystallization; D018360:Crystallography, X-Ray; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D000097793:Legumins
D010940:Plant Proteins; D000097793:Legumins; C007578:edestin protein, Cannabis sativa