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. 2012 Jun 25;40(17):8721–8732. doi: 10.1093/nar/gks611

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© The Author(s) 2012. 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/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Overall structure of Zfp206SCAN. (A) The Zfp206SCAN domain-swapped dimer is formed by packing helix H2 of one monomer (green) against helices H3 and helix H5 of the opposing monomer (orange). (B) The (2F_O-F_C) map of the dimer interface involving residues Arg13 and Arg31 in molecule 1 and Gln56 and Glu50 (as indicated in Figure 2A) in molecule 2 of Zfp206SCAN contacted by hydrogen bond. The electron density (2F_o-F_c) is displayed at the 0.5σ level. (C) The (2F_O-F_C) map of the dimer interface involving residues Ile48 and Leu49 in molecule 1 and Cys34, Ile48 and Leu49 of molecule 2 (as indicated in Figure 2A).