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. Author manuscript; available in PMC: 2009 Jan 1.
Published in final edited form as: Nat Struct Mol Biol. 2008 Jun 22;15(7):738–745. doi: 10.1038/nsmb.1448

Figure 3.

Figure 3

Structure-guided mutagenesis of the active site. (a) Kinetics for 30 nM of Rtt109–Vps75 complex with saturating levels of acetyl-CoA (25 μM) and full-length histone H3 at specified concentrations. The averages of two duplicate experiments are shown for each data point. The solid line is fit to the Hill equation, and the dashed line is fit to the classical Michaelis-Menten equation (see Methods). (b) Kinetics for 30 nM of Rtt109 W222F–Vps75 mutant complex with 21 μM of acetyl-CoA and full-length histone H3 at specified concentrations. (c) Kinetics for 30 nM of Rtt109 D287A–Vps75 mutant complex with 21 μM of acetyl-CoA and full-length histone H3 at specified concentrations. (d) The table summarizes the kinetic parameters measured in Figure 3a–c and Supplementary Figure 5. N.D., not determined due to experimental considerations.