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. 2018 Jul 20;9:2844. doi: 10.1038/s41467-018-05251-z

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Signatures of single myosin-5B molecule motility under unloaded condition. a The velocity of myosin-5B movement (n = 127) on F-actin increases with increasing ATP following Michaelis–Menten kinetics (red curve), with v_max = 691 ± 25 nm s⁻¹ and K_app = 22 ± 2 µM. Error bars, s.d. b The run length (n = 127) is ATP-independent within error bars. Average run length is 780 ± 2 nm (red line). Error bars, s.d. c Representative time trace of myosin-5B stepping forward in discrete 36 nm increments on the actin filament. Average step 36 ± 4 nm (n = 42, s.e.m., [ATP] = 0.3 µM)