XB-ART-11520
Acta Crystallogr D Biol Crystallogr
2000 Feb 01;56Pt 2:212-4. doi: 10.1107/s0907444999016054.
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Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein.
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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 A resolution. The space group was determined to be P6(1)22 or P6(5)22, with unit-cell dimensions a = b = 95.9, c = 93.9 A.
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Species referenced: Xenopus laevis
Genes referenced: dvl2