Crystallization and crystal data on tyrosine phenol-lyase

FEBS Lett. 1988 May 23;232(2):381-2. doi: 10.1016/0014-5793(88)80774-9.

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.

MeSH terms

  • Ammonium Sulfate
  • Apoenzymes*
  • Apoproteins*
  • Chemical Precipitation
  • Citrobacter / enzymology*
  • Crystallization
  • Hydrogen-Ion Concentration
  • Lyases*
  • Macromolecular Substances
  • Polyethylene Glycols
  • Tyrosine Phenol-Lyase*
  • X-Ray Diffraction

Substances

  • Apoenzymes
  • Apoproteins
  • Macromolecular Substances
  • Polyethylene Glycols
  • Lyases
  • Tyrosine Phenol-Lyase
  • Ammonium Sulfate