G protein-coupled receptors are important drug targets because of their roles in a wide spectrum of biological processes. CCR5, for example, is the principle co-receptor for transmission of HIV. However, efforts to screen for inhibitors of these receptors are often hampered by their tendency to unfold when extracted from their native membranes. On page 649, Mirzabekov and coworkers describe a method in which CCR5 is affixed to paramagnetic beads and surrounded with lipids, while retaining its native conformation. First they coated magnetic beads with streptavidin and an antibody that recognizes a tag on CCR5. They then used the beads to capture CCR5 from cell lysates, and the protein was reconstituted with detergent-solubilized lipids right on the bead. To demonstrate the utility of the approach, they used the beads to select CCR5-specific antibodies from a recombinant phage display library.