We report that a symmetric small molecule ligand mediates assembly of the antibody light chain variable domains (V L s) into a corresponding symmetric ternary complex with novel interfaces. L5* Fluorogen Activating Protein (FAP) is a VL domain that binds malachite green (MG) dye to activate intense fluorescence. Crystallography of liganded L5* reveals a 2:1 protein:ligand complex with extensive C2 symmetry, with MG almost completely encapsulated between an antiparallel arrangement of the two VL domains. Unliganded L5* VL domains crystallize as … Continue reading „Malachitgrüner konjugierter Antikörper“