Copyright information:Taken from "Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery"Nucleic Acids Research 2006;34(8):2186-2195.Published online 28 Apr 2006PMCID:PMC1450331.© The Author 2006. Published by Oxford University Press. All rights reserved0) with ATPγS (5 mM) in the same buffer. Titration was performed at 27°C with a reference power of 15 µcal/s. Injection volume was 10 µl. () Represents the change in reference power (µcal/s) with respect to time. () Represents the heat exchange per mole (kcal/mol) of ATPγS added. The curve obtained was fitted using software Origin 7.0 with one set of binding sites. The value of N, K, ΔH and ΔS obtained were 4.78, 4.14 × 10 M, −238 kcal moland 20.3 kcal molk, respectively.