Dynamic proteins and multi-protein complexes govern most biological processes. Cross-linking/mass spectrometry (CLMS) is increasingly successful in providing residue-resolution data on static proteinaceous structures. In order to investigate the technical feasibility of recording dynamic processes using isotope-labelling for quantitation, we generated a model dataset by cross-linking human serum albumin (HSA) with the readily available cross-linker BS3-d0/d4 in different heavy/light ratios.