Discovering and characterizing protein–protein interactions (PPIs) that contribute to cellular homeostasis, development, and disease is a key priority in proteomics. Numerous assays for protein–protein interactions have been developed, but each one comes with its own strengths, weaknesses, and false-positive/false-negative rates. Therefore, it seems rather intuitive that combining multiple assays is beneficial for robust and reliable discovery of interactions. Along those lines, in their recent study, Wanker and colleagues (Trepte et al, 2018) combined two complementary and quantitative interaction assays in one pot. One assay is luminescence-based and depends on protein proximity in living cells, while the other relies on formation of more stable complexes detected by co-precipitation with a luminescence-based readout, which facilitates confident identification and quantitation of interactions in high throughput.