Crystallographic studies on L-asparaginase from Proteus vulgaris. II. Symmetry and location of the tetrameric molecule.
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.
D001215:Asparaginase; D046911:Macromolecular Substances; D011487:Protein Conformation; D011514:Proteus vulgaris / Q000201:enzymology*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D001215:Asparaginase