Abstract
Affinity purification is a powerful tool that has become a prime choice as capture step in membrane protein purification. Recombinant membrane proteins are commonly purified by use of polyhistidine tags and immobilized metal affinity chromatography (IMAC).The combination of magnetic beads and IMAC resins (pre‐charged with Ni2+‐ions) allows for an easy‐to‐use format for rapid, small‐scale, screening of conditions optimal for purification of membrane proteins.Screening for optimal purification conditions for a number of integral membrane proteins was performed. Vital parameters as choice of detergent, wash and elution buffer concentrations etc were addressed. All experiments were done using Ni2+‐charged chromatography media on magnetic beadsThe magnetic bead format simplified and shortened the handling procedures through‐out the screening workflow. Obtained results from screening for several detergents gave reliable results that could be fed into further scale‐up experiments.
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