Extended Data Fig. 8: Donor specificity of GalS1 and β-1,4-galactotetraose acceptor dissociation constants (KD) of GalS1 WT and its variants.
From: Structural and biochemical insight into a modular β-1,4-galactan synthase in plants

a, Sugar-nucleotide specificity of GalS1. Reactions were carried out using 0.1 mM of UDP-substrate with 4 µg of the GalS1 enzyme in 50 mM HEPES, pH 7.5 in the absence of acceptor substrate. The values shown are mean values (bar) ± standard deviation (error bars) of a representative experiment for n = 3 technical replicates (red circles) and plotted using GraphPad Prism 9.5.0. b, Comparison of dissociation constants (KD) of PtGalS1 WT and its variants predicted for β-1,4-galactotetraose acceptor binding by microscale thermophoresis (MST). The values shown are mean values (filled circles) of the KD obtained after using KD fit model in the MO.Affinity Analysis software (NanoTemper Technologies) ± KD confidence (error bars). Error Bars represent standard deviation confidence (SD) values defined by the range where the KD falls with 68% of certainty, each point represents the mean of six sets of measurements (n = 6).