For colchicines, the drugs interact with both α-tublin and β-tublin which in fact form a hetrodimer. As shown in the figure beside, the sky-blue stick structure buried in the gray and pink protein surface of the α-tublin and β-tublin heterodimer is the crystal structure of colchicine. Because of interaction with colchicines, the conformation of tublins formed is not straight and will interfere with the polymerization of tublin-α-β. We have applied our docking approach to examine if this structure is reproducible. The docked structure of colchicine is represented by blue stick and the root-mean squared difference (RMSD) between coordinates of docked and x-ray crystal structure is 1.15 A. This docking result shows that the interaction between docked drug and protein is well reserved as compared with that of the x-ray structure. This serves as an example of our effort to apply the virtual screening technique to search some known drug databases to recover drugs that might be functional to against some otherwise intangible diseases. In short, searching new usages for old drugs is the paramount goal of our company and we shall do our best to exploring it.