view article

Figure 2
RBD Q498Y–ACE2 binding kinetics determined by biolayer interferometry (BLI). (a) ACE2 was captured on the surface of an Ni–NTA sensor and pulsed for 2 min with increasing concentrations of RBD wt, RBD Q498Y or RBD β in running buffer (20 mM HEPES pH 7.4, 150 mM NaCl). The association and dissociation data were monitored and fitted to a 1:1 Langmuir model for the calculation of binding kinetics constants (kon, koff and Kd) and assessment of the goodness of fit (R2). The signal corresponding to the buffer was subtracted prior to any calculations. Colored lines represent experimental raw data and black lines the binding kinetics fittings.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds