Expression, purification, crystallization and preliminary X-ray diffraction analysis of human uroporphyrinogen decarboxylase.
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.
Unité de Biophysique Structurale, EP534-CNRS, Université Bordeaux 1, Talence, France.
M
M
Laterrière
B L
BL
d'Estaintot
A
A
Dautant
G
G
Précigoux
I
I
Hombrados
H
H
De Verneuil
D003460:Crystallization; D004926:Escherichia coli; D015870:Gene Expression; D006801:Humans; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014575:Uroporphyrinogen Decarboxylase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D014575:Uroporphyrinogen Decarboxylase