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 Å and γ=116° having an equivalent triply centered hexagonal cell of a=b=215 Å, c=80 Å. 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. © 1994 Academic Press Limited.