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. 2021 Feb 1;153(3):e202012726. doi: 10.1085/jgp.202012726

Figure S9.

Figure S9.

Comparison of radial intensity profile of MyBP-C fluorescence from the center of the actin hexagon in active sarcomeres to in silico models with MyBP-C bound to myosin, when myosin is bound to actin. (A) Illustrative representations of MyBP-C bound to myosin, which is attached to actin. (B) Theoretical model generated using the high-resolution cryo-EM structure of myosin (grey and blue) bound to an actin thin filament (green and grey) in rigor (PDB accession no. 5H53). MyBP-C’s C0 domain (orange; from PDB accession no. 6CXI) with an antibody (magenta; PDB accession no. 1IGT) was placed in close proximity to the RLC (blue) attached to myosin heavy chain (grey) based on in vitro structural evidence (Ratti et al., 2011). The pink stars indicate the centroid position of the fluorophores attached to the antibody. (C) White areas are target zones for random placement of the fluorophores for when MyBP-C is bound to myosin with myosin bound to actin, as shown in A, for in silico models. (D) Red areas are regions of the image in which fluorophores cannot be randomly placed due to steric exclusion from the myosin and actin filaments. (E) Average in silico reconstructed images generated with a fraction of the fluorophores bound to myosin when myosin is bound to actin and the remaining fluorophores are randomly distributed throughout the image, except for red areas shown in C. Each image is an average of 120 individual simulations. Scale bar, 25 nm. (F) The radial intensity profiles for the position of MyBP-C relative to the center of the average actin hexagon in the active sarcomere and in silico images shown in E; color scheme as in Fig. S6 F. a.u., arbitrary unit.