Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein

Dishevelled (Dsh) protein is an important component of the Wnt signal-transduction pathway. It has three relatively conserved domains: DIX, PDZ and DEP. The PDZ domain of the Xenopus laevis homolog of Dsh, which consists of residues 254-348, was overexpressed as a soluble protein in Escherichia coli, purified and crystallized. The crystals were obtained by the vapor-diffusion method, using 1.4 M sodium formate as a precipitant. The crystals diffracted to 2.3 Å resolution. The space group was determined to be P6₁22 or P6₅22, with unit-cell dimensions a = b = 95.9, c = 93.9 Å.