The correct folding of solubilized recombinant proteins is of key importance for their production in industry. On‐column refolding of proteins is mainly achieved by three methods: size‐exclusion chromatography, ion exchange chromatography and affinity chromatography using immobilized metal chelates. The principles of these methods were first laid down in the 1990s, but many recent improvements have been made to these processes. Immobilized metal‐ion affinity chromatography (IMAC) represents a relatively new separation technique that is primarily appropriate for the purification of proteins with natural surface‐exposed histidine residues and for recombinant proteins with engineered histidine tags or histidine clusters. Because the method has gained broad popularity in recent years, the main recent developments in the field of new sorbents, techniques and possible applications are discussed in this article.