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Crystallographic characterization and molecular symmetry of edestin, a legumin from hemp.

  • Author(s): Patel, S
  • Cudney, R
  • McPherson, A
  • et al.
Abstract

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.

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