MST analysis of the binding of anti-
Nb84 with the purified MOMP monomer. The binding curve of Nb84 with the MOMP monomer was obtained in a saturation binding experiment. The formation of Nb84-MOMP complexes was measured at constant concentrations of the fluorescently labelled Nb84 (32 nM) and varying concentrations of unlabelled MOMP (0.3 nM–5 µM). Data were normalized to ΔFnorm [‰]. The competitive binding curves visualise the inhibition of binding of the fluorescently labelled Nb84 (32 nM) with MOMP (0.3 nM–5 µM) by unlabelled A Nb5, B Nb22 and C Nb84 (10 µM). The error bars represent the standard deviations.