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. Author manuscript; available in PMC: 2011 Jan 15.
Published in final edited form as: Bioorg Med Chem. 2009 Nov 20;18(2):896. doi: 10.1016/j.bmc.2009.11.033

Figure 3. Assay optimization.

Figure 3

Km determinations of (A) TDP-KDX and (B) NADPH. Substrate versus rate plots are shown; Km values were determined from these data as described in materials and methods. (C) Determination of the IC50 of the known inhibitor TDP used for quality control. (D) HTS quality control plate; Z′ was calculated to be 0.78. The data with fluorescence values of ~200,000 were controls with full activity (with no TDP); the data points with values of ~0 were blanks with no activity (contained no TDP-KDX); and the data points at ~75,000 were positive controls for inhibition (containing TDP-KDX, NADPH, RmlC and TDP at a concentration of 500 μM). (E) Z′-values of HTS plates.