Crystallization and crystal data on tyrosine phenol-lyase.
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.
Demidkina
T V
TV
Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Myagkikh
I V
IV
Antson
A A
AA
Harutyunyan
E H
EH
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
D001051:Apoenzymes; D001059:Apoproteins; D046911:Macromolecular Substances; D011092:Polyethylene Glycols; D008190:Lyases; D014447:Tyrosine Phenol-Lyase; D000645:Ammonium Sulfate