Supplementary Figure 2: Fluorescence anisotropy-based affinity measurements of zUSP30 or Lys6-Ub2 mutants. | Nature Structural & Molecular Biology

Supplementary Figure 2: Fluorescence anisotropy-based affinity measurements of zUSP30 or Lys6-Ub2 mutants.

From: Structural basis for specific cleavage of Lys6-linked polyubiquitin chains by USP30

Supplementary Figure 2

Error bars represent the standard deviations from the mean values of measurements performed in triplicate. The data were fitted to a one-site binding model to derive dissociation constants (Kd). (a) Fluorescence anisotropy-based affinity measurements of zUSP30 (C73A) mutants with Lys6-Ub2. Fluorescence polarization values are plotted as a function of the concentration of each zUSP30 (C73A) mutant. (b) Fluorescence anisotropy-based affinity measurements of zUSP30 (C73A) with Lys6-Ub2 mutants. Fluorescence polarization values are plotted as a function of the concentration of zUSP30 (C73A). (c) Summary of affinity measurements. Data are presented as mean ± standard deviation. Asterisks indicate that the actual Kd is above half of the upper limit of the substrate concentration (more than 20 μM).

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