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Updated: Aug 1, 2026
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Expression, purification, crystallization and preliminary X-ray diffraction analysis of human uroporphyrinogen
M Laterrière1, B L d'Estaintot, A Dautant
1Unité de Biophysique Structurale, EP534-CNRS, Université Bordeaux 1, Talence, France.
Abstract:
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.
