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  • Title: Crystallographic studies on L-asparaginase from Proteus vulgaris. II. Symmetry and location of the tetrameric molecule.
    Author: Lee B, Yang HJ, Henry GM, Seymour JP, Chibata I.
    Journal: J Biol Chem; 1975 Aug 25; 250(16):6228-31. PubMed ID: 1099088.
    Abstract:
    Analyses of the x-ray diffraction intensity data by the Patterson synthesis and rotation function techniques show that the true space group of the monoclinic crystals of L-asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) from Proteus vulgaris is P21, that the molecular centers lie at x = 0.054, y = 0, z = 0.256, and its symmetry related positions, and that the tetramer molecules possess three approximate, mutually perpendicular 2-fold rotational symmetries, the axes of which run along the directions of the crystallographic a*-, b-, and c-axes. In addition, an investigation of the molecular packing arrangement in the crystal indicates that the tetramer molecules possess an approximately regular tetrahedral subunit structure.
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