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. Author manuscript; available in PMC: 2017 Aug 22.
Published in final edited form as: Curr Biol. 2016 Aug 4;26(16):2202–2207. doi: 10.1016/j.cub.2016.06.029

Table 1.

Summary of single molecule parameters

Construct Track [KCl] (mM) Run length (µm)a Speed (µm/sec)b N
Single motor motilityc
   MyoVc Actin 25 No runs No runs 0
   MyoVa Actin 25 0.48 ± 0.02 0.48 ± 0.21 182
   VcVa chimera Actin 25 0.18 ± 0.004 0.54 ± 0.21 182
   MyoVc Actin bundles 25 0.49 ± 0.10 0.44 ± 0.23 207
   MyoVc, 37°C Actin bundles 25 1.26 ± 0.02 0.54 ± 0.34 206
Multiple motor motilityd
   MyoVc Actin 25 0.26 ± 0.02 0.13 ± 0.10 108
   MyoVc Actin 150 No runs No runs 0
   MyoVc Actin bundles 150 0.35 ± 0.02 0.16 ± 0.13 203
a

The characteristic run length (λ) was obtained by fitting the cumulative frequency histogram to an exponential function. Error is in standard error of the fit. No runs detected, with a minimum detectable run length of 120 nm.

b

Mean ± SD.

c

Mixing ratios of 1 myosin dimer per 5–10 Qdots ensures that the majority of Qdots are bound by a single motor. Experiments were performed at 1 mM MgATP and 22°C unless specified.

d

Mixing ratios of 10 myosin dimers per 1 Qdot promotes the recruitment of multiple MyoVc motors per Qdot.