Laterrière M, d'Estaintot B L, Dautant A, Précigoux G, Hombrados I, De Verneuil H
Unité de Biophysique Structurale, EP534-CNRS, Université Bordeaux 1, Talence, France.
Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):476-8. doi: 10.1107/s090744499701250x.
A recombinant human uroporphyrinogen decarboxylase (E.C. 4.1.1.37, UROD) has been expressed in Escherichia coli and purified to homogeneity. Crystals grew by the hanging-drop vapor-diffusion technique from a starting solution containing 1.5 mg ml-1 protein. The crystals belong to the trigonal space group P3121 or its enantiomer P3221 and diffract to 3 A resolution. The unit-cell parameters are a = b = 103.4, c = 75.7 A and gamma = 120 degrees. The asymmetric unit contains one molecule. Preliminary structural predictions suggest for the protein a TIM-barrel type tertiary structure.
