A chromatographic method for the purification of (His)₆ -tagged recombinant proteins expressed as inclusion bodies in Escherichia coli is described. The inclusion bodies are solubilized in 8 M urea and bound to a Ni ²⁺ -charged HiTrap™ Chelating HP column. On-column refolding of the bound proteins is performed by buffer exchange of the bound proteins from a buffer containing 8 M urea to a non-denaturing buffer (0 M urea) using a linear gradient. Finally, bound proteins are eluted with a step gradient of imidazole. The method has been successfully used for the purification of two recombinant Schistosoma mansoni proteins.