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. 2009 Mar 2;37(7):2395–2404. doi: 10.1093/nar/gkp092

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© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Binding isotherms for the interaction of Bst DnaB with DnaI-N domain constructs, as measured by SPR. Experimental points obtained with: DnaI-N132 (filled circle), DnaI-N123 (filled square) and DnaI-N106 (filled triangle). The K_D values for these interactions, determined by the least squares fit to a 1:1 binding model (solid lines) are: DnaI-N132, 0.65 μM; DnaI-N123, 7.3 μM; DnaI-N106, 18.5 μM. Given the difference in the K_D values, different ranges of protein concentrations were used: DnaI-N132, 0.1–1 μM; DnaI-N123, 0.1–20 μM; DnaI-N106, 0.1–60 mM. The responses (R, in RU) were normalized using the computed value of the maximum response at equilibrium (R_max), which corresponded to 0.8, 1.7 and 1.8 molecules of DnaI-N132, DnaI-N123 and DnaI-N106, respectively, bound per Bst DnaB subunit.