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Multivalent carbohydrate-lectin interactions are a key concept in biological processes mediating, e.g., signaling and adhesion. Binding affinities of multivalent ligands often increase by orders of magnitude compared to a monovalent binding situation. Thus, the design of multivalent ligands as potent inhibitors is a highly active field of research, where knowledge about the binding site topology is crucial. Here, we report a general strategy for precise distance measurements between the bindingdoi:10.1021/acs.jpclett.8b02243.s001 fatcat:akquq37lobd5zm2vgner6e6s5y