Extended Data Fig. 5: Additional information on SAXS-based Khc modeling.
From: Tropomyosin 1-I/C coordinates kinesin-1 and dynein motors during oskar mRNA transport
a, Template model of Khc used for randomization. Coordinates of the structured parts (motor domain: residues 1–378; four coiled-coil regions: residues 403–585, 604–706, 711–838 and 844–936) were generated by AF245,46 and connected with the coordinates of the missing linker residues. b, χ2 distribution of all Crysol fits to the Khc (left) and Khc-Tm1 (right) scattering curves. c, Best (upper panel) and mediocre (lower panel) fits of Khc (left) and Khc-Tm1 (right) structural models to the experimental scattering curves. d, Alignments of the five best fits for Khc (left) and for Khc-Tm1 (right). e, Close-ups of the AMB domains in the four best fitting models for Khc. f, Close-ups of the AMB domains in the four best fitting models for Khc-Tm1. Khc models are shown in shades of blue with the AMB domains marked in red; Tm1 is shown in shades of pink.
