Dvl (Dishevelled) is a key effector molecule of the Wnt signaling pathway. The DIX domain of Dvl (Dvl-DIX) can homo-oligomerize into cytoplasmic puncta via the intra-filament SiteⅠ, SiteⅡ and the inter- filament SiteⅢ, and form hetero-complex with the DIX domain of Ccd1 (Ccd1-DIX) through SiteⅠ and SiteⅡ. Since all efforts to solve the wildtype Dvl2-DIX structure were unsuccessful, we carried out crystallization trials with the SiteⅢ mutants of Dvl2-DIX that display impaired homo-oligomerization and Wnt activity. Crystals of Dvl2-DIX(G65A) protein were obtained, but the diffraction data encountered an unexpected lattice-translocation defect. These SiteⅢ mutations of Dvl2-DIX retained the ability to hetero-interact with Ccd1-DIX, and we thus successfully generated various complexes between Dvl2-DIX mutants and wildtype Ccd1-DIX. After extensive trials, crystals of the Dvl2-DIX(G65A)-Ccd1-DIX complex were produced, but of poor quality and unsuitable for diffraction studies. Optimization is under way.