Immobilized-metal affinity chromatography is presented in this paper as a powerful technique for recombinant protein purification. The development of this method and some recommendations for potential users are also described. Recombinant proteins with fused oligohistidine tags can be purified to homogeneity under native or denaturing conditions. In some cases, denatured immobilized proteins can be directly refolded in a matrix-assisted procedure. It is also possible to use immobilized recombinant proteins for the isolation of specific antibodies or other molecules. In future, we can expect special bacterial strains to be developed for oligohistidine-tagged protein expression and improved design of affinity tags.