Heterogeneous distribution of kinesin-streptavidin complexes revealed by mass photometry

Kinesin-streptavidin complexes are widely used in microtubule-based active-matter studies. The stoichiometry of the complexes is empirically tuned but experimentally challenging to determine. Here, mass photometry measurements reveal heterogenous distributions of kinesin-streptavidin complexes. Our binding model indicates that heterogeneity arises from both the kinesin-streptavidin mixing ratio and the kinesin-biotinylation efficiency., , , # Data from: Heterogeneous distribution of kinesin-streptavidin complexes revealed by Mass Photometry

[https://doi.org/10.5061/dryad.1rn8pk12h](https://doi.org/10.5061/dryad.1rn8pk12h)

Data underlying Figs. 2-4 and Figs. S1-S10.

## Description of the data and file structure

Data underlying Figs. 2-4, Fig. S1, Figs. S2b-S6b, and Figs. S7b-S10 are provided in .xlsx file format. Data underlying Figs. S2a and S7a  are provided in .tif file format. Details below:

* **Figure 2.xls:**  data underlying Fig. 2 in the main text. This file contains three tabs.
* MassPhotometry Counts Tab:
* Column A: Mass (kDa)
* Column B: Counts of Kinesin (K)
* Column C: Counts of Streptavidin (S)
* Column D: Counts of K:S 0.4:1
* Column E: Counts of K:S 0.8:1
* Column F: Counts of K:S 1.6:1
* Column G: Counts of K:S 2.2:1
* Column H: Counts of K:S 3.0:1
* Column I: Counts of K:S 3.6:1
* Global Fit (red l...