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. 2017 Sep 13;45(21):12170–12180. doi: 10.1093/nar/gkx812

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — The B-domain of TRF2 becomes rigid upon binding to telomeric DNA duplex. Kratky plots (I*q² versus q) of the unbound B-domain (A) and B-domain in complex with telomeric DNA duplex (B). Scattering data from the unbound B-domain (A) exhibit increase characteristic for macromolecules with substantial flexible or unstructured regions, while scattering data from the B-domain–DNA complex (B) display clear minimum characteristic for well-folded compact particles. (C) The typical MONSA model of the B-domain–DNA complex. The DNA phase (mesh) is superimposed with molecular model of telomeric DNA duplex. The protein phase (spheres) illustrates the bound B-domain as a compact body. Fits of simulated scattering to experimental data: (D) DNA phase with final χ² value 1.22. (E) B-domain–DNA complex phase with χ² value 1.06.