Supplementary Figure 5: Structural analysis of PAR1 reconstituted in proteoliposomes.
From: Imaging G protein–coupled receptors while quantifying their ligand-binding free-energy landscape
(a) Topography of PAR1s sparsely distributed in lipid membranes made of 0.5 mg mL−1 DOPC and 0.05 mg mL−1 CHS. Histogram of diameter (b) and height (c) of PAR1 particles imaged in (a). (b) The diameter distribution showed two peaks centered at 8.1 ± 1.3 nm (average ± S.D.) and 14.7 ± 0.6 nm. Diameters were measured at full-width half maximum of particle heights. (c) The height distribution showed two peaks centered at 1.2 ± 0.2 nm (average ± S.D.) and 2.0 ± 0.3 nm, which could correspond to the height of the extracellular or intracellular surface emerging from the DOPS/CHS membrane, respectively (d). The FD-based AFM topograph was recorded in imaging buffer (300 mM NaCl, 20 mM Hepes, 25 mM MgCl2, pH 7.0) at room temperature. n gives the number of PAR1 particles analyzed.
