Supplemental data for 'Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization''

<strong>Supplemental mass photomerty raw data used in Figure 3</strong> of 'Guaitoli, G., Zhang, X., Saitta, F., Miglionico, P., Silbermann, L.M., Ho, F.Y., Zweydorf, F.v., Signorelli, M., Tych, K., Fessas, D., Raimondi, F., Kortholt, A., and Gloeckner, C.J. (2023). Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization. <em>bioRxiv</em>, 2023.2008.2011.549911 doi: 10.1101/2023.08.11.549911' <strong>Raw data Figure 3A:</strong> Mass photometry raw data for LRRK2 wild-type in presence of different G-nucleotides at different LRRK2 concentrations. Three biological replicates have been considered for the statistical analysis. <strong>Raw data Figure 3B: </strong>Mass photometry raw data for LRRK2 WT (left panel), LRRK2 WT + MLi-2 (middle panel) and kinase-dead LRRK2 (right panel) without and with ATP pre-incubation (-/+ ATP). Two biological and three technical replicates have been considered for the statistical analysis. <strong>Raw data Figure 3C</strong><strong>:</strong> Mass photometry raw data for pathogenic LRRK2 variants in presence of different G-nucleotides. Two biological and two technical replicates have been considered for the statistical analysis<strong>.</strong>