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. 2014 Jan 1;25(1):66–75. doi: 10.1091/mbc.E13-04-0200

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© 2014 Clayton et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — Myo52p molecules lacking their cargo-binding domain undergo efficient motility along actin cables. (A) Time-lapse montages showing directed movement of full-length Myo52p-3xGFP (top) and truncated Myo52pΔCBD-3xGFP (bottom) particles in wild-type myo52-3xGFP and myo52ΔCBD-3xGFP cells, respectively (after growth on YE5S rich medium at 25°C). Directed movements were captured over time using TIRF microscopy. Far right, maximum projections of the particle trajectories. Bar, 4 μm. Representative events from the myo52ΔCBD-3xGFP strain are also presented in Supplemental Movie S5. (B) Histogram of the speed distribution of full-length Myo52p and Myo52pΔCBD particles. (C, D) Average run length (n = 45 in C) and event frequency (cell number = 82–122 in D) of motile Myo52p and Myo52pΔCBD particles. (E) Histogram of Myo52pΔCBD GFP intensity as number of dimeric motors/motile particle.