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 Å resolution. The unit-cell parameters are a = b = 103.4, c = 75.7 Å and γ = 120°. The asymmetric unit contains one molecule. Preliminary structural predictions suggest for the protein a TIM-barrel type tertiary structure.