title: Crystallization and crystal data on tyrosine phenol-lyase.
abstract: Crystals of the apoenzyme of tyrosine phenol-lyase (EC 4.1.99.2), a pyridoxal 5'-phosphate-dependent enzyme from Citrobacter intermedius, have been grown by vapor diffusion of an ammonium sulfate solution to a protein solution. The crystals belong to space group P2(1)2(1)2, with dimensions of a = 75.5 A, b = 138.4 A and c = 94.1 A and diffract up to 2.7 A resolution. The asymmetric unit contains one half of the enzyme tetrameric molecule. Two heavy-atom derivatives of the crystals have been obtained.
authors: Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
authors: T V
authors: TV
authors: Demidkina
authors: I V
authors: IV
authors: Myagkikh
authors: A A
authors: AA
authors: Antson
authors: E H
authors: EH
authors: Harutyunyan
mesh_terms: D000645:Ammonium Sulfate; D001051:Apoenzymes; D001059:Apoproteins; D011232:Chemical Precipitation; D002954:Citrobacter / Q000201:enzymology*; D003460:Crystallization; D006863:Hydrogen-Ion Concentration; D008190:Lyases; D046911:Macromolecular Substances; D011092:Polyethylene Glycols; D014447:Tyrosine Phenol-Lyase; D014961:X-Ray Diffraction
chemical_list: D001051:Apoenzymes; D001059:Apoproteins; D046911:Macromolecular Substances; D011092:Polyethylene Glycols; D008190:Lyases; D014447:Tyrosine Phenol-Lyase; D000645:Ammonium Sulfate