Preliminary crystallographic data for glycolate oxidase from spinach.
Glycolate oxidase, an enzyme that plays an important role in photorespiration in plants, has been purificant from spinach and crystallized in two different crystal forms. Form A which was obtained with tertiary butanol as precipitating agent belongs to space group I 422 with unit cell dimensions a = b = 148.1 A and c = 134.9 A. This form diffracts to high resolution and will be used for further crystallographic studies. Form B is also tetragonal, space group P42212, with cell dimensions a = b = 145.4 A and c = 104.2 A. This form was obtained from ammonium sulfate precipitations. Sodium dodecyl sulfate polyacrylamide gel electrophoresis shows that the enzyme is built up from subunits of molecular weight 37,000. The asymmetric units of both crystal forms contain at least two such subunits.
D000429:Alcohol Oxidoreductases; D006016:Glycolates; D046911:Macromolecular Substances; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D006016:Glycolates; D046911:Macromolecular Substances; D000429:Alcohol Oxidoreductases; C020821:glycollate oxidase