Here, we share image stacks acquired under total internal reflection fluorescence (TIRF) microscopy and representative trajectories of single myosin-5B molecules labelled with Quantum Dots (QD-myo-5B) moving along actin filaments at different ATP concentrations (0.3-1000 mM). Localization of QD-myo-5B was performed with the PROOF software, which is freely available [1]. The data can be valuable for researchers interested in molecular motors motility, both from an experimental and modeling point of view, as well as to researchers developing single particle tracking algorithms. The data is related to the research article "Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level" Gardini et al., 2015. (c) 2019 The Authors. Published by Elsevier Inc.

Myosin-5B is one of three members of the myosin-5 family of actin-based molecular motors fundamental in recycling endosome trafficking and collective actin network dynamics. Through single-molecule motility assays, we recently demonstrated that myosin-5B can proceed in 36-nm steps along actin filaments as single motor. By analyzing trajectories of single myosin-5B along actin filaments we showed that its velocity is dependent on ATP concentration, while its run length is independent on ATP concentration, as a landmark of processivity.

Myosin V fluorescence imaging dataset for single-molecule localization and tracking

Gardini Lucia;Pavone Francesco Saverio;
2019

Abstract

Myosin-5B is one of three members of the myosin-5 family of actin-based molecular motors fundamental in recycling endosome trafficking and collective actin network dynamics. Through single-molecule motility assays, we recently demonstrated that myosin-5B can proceed in 36-nm steps along actin filaments as single motor. By analyzing trajectories of single myosin-5B along actin filaments we showed that its velocity is dependent on ATP concentration, while its run length is independent on ATP concentration, as a landmark of processivity.
2019
Istituto Nazionale di Ottica - INO
Inglese
25
103973
103973
4
http://www.scopus.com/inward/record.url?eid=2-s2.0-85066448077&partnerID=q2rCbXpz
Sì, ma tipo non specificato
Here, we share image stacks acquired under total internal reflection fluorescence (TIRF) microscopy and representative trajectories of single myosin-5B molecules labelled with Quantum Dots (QD-myo-5B) moving along actin filaments at different ATP concentrations (0.3-1000 mM). Localization of QD-myo-5B was performed with the PROOF software, which is freely available [1]. The data can be valuable for researchers interested in molecular motors motility, both from an experimental and modeling point of view, as well as to researchers developing single particle tracking algorithms. The data is related to the research article "Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level" Gardini et al., 2015. (c) 2019 The Authors. Published by Elsevier Inc.
Total internal reflection fluorescence (TIRF) microscopy
Myosin
Single molecule biophysics
This work was supported by the European Union's Horizon 2020 research and innovation program under grant agreement no. 654148 Laserlab-Europe and by Ente Cassa di Risparmio di Firenze.
4
info:eu-repo/semantics/article
262
Gardini, Lucia; Arbore, Claudia; Pavone, FRANCESCO SAVERIO; Capitanio, Marco
01 Contributo su Rivista::01.01 Articolo in rivista
none
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/379850
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