Fig. 6
From: Structural and functional consequences of the STAT5BN642H driver mutation
FP binding assays and denaturation temperatures of STAT5B /STAT5BN642 mutants. a The fluorescence polarization of 10 nM fluorescently labeled peptide was measured from samples containing increasing concentrations of wild-type/mutant STAT5B and the dissociation constants were determined from curve-fitting to a 1:1 protein-ligand model. The error bars show the mean ± SD from three independent titrations, and the Kd is reported with the error in the fit. b The denaturation temperatures of 2.5 µM STAT5B and STAT5BN642 mutants were determined at different pH values in the presence or absence of 50 µM peptide. The melting temperature is reported as the average from three independent samples and the error bars show the mean ± SD. Source data are provided as a Source Data file
