Microtubule conformational changes examined with cryo-EM. (A) The estimated resolutions according to the Fourier shell correlation 0.143 criteria, and pitch distances for tubulin dimer calculated from the helical symmetry parameters. (B) Cryo-EM reconstruction of KIF5C(PNP)–MT(GDP) and the docked atomic model showing only the microtubule surface. (C) Cα chain trace models of KIF5C(PNP)–MT(GDP) and KIF5C(ø)–MT(GDP) superimposed at α-tubulin on the right end. Note the tilt angle changes (1.1°) at the intradimer interface, which leads to the extension of the pitch (1.0 Å). Tubulin subunits and KIF5C in KIF5C(PNP)–MT(GDP) are shown in cyan and blue, and those in KIF5C(ø)–MT(GDP) are shown in green. Helices and loops involved in the rearrangement of lattice are highlighted in red. (D) The Cα chain trace model of KIF5C(ø)–MT(GDP) colored by root mean square deviation values between the Cα atoms in C, viewing from the left side and the right side. The interface elements of KIF5C were highlighted as in C. See Fig. S4 for resolution and the statistics of cryo-EM maps.