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. 2010 Feb 5;38(10):3209–3221. doi: 10.1093/nar/gkq026

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Binding of recombinant MSL2 to different DNA fragments in vitro. Electrophoretic mobility shift assay. Increasing concentrations of MSL2 were incubated with radiolabeled dsDNA of (A) the high-affinity DBF12-L15 element and the mutated version DBF12-L18 or (C) the DBF12-L15 trimer and a random fragment of similar length derived from the multiple cloning site of a vector (mcs). Protein–DNA complexes were separated from unbound DNA in non-denaturing agarose gels. (B) and (D) Binding curves obtained from quantification of (A) and (C) and fitting to a standard bimolecular model.