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. 2014 Mar 1;28(5):451–462. doi: 10.1101/gad.236745.113

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© 2014 Roset et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.

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Figure 1. — Analysis of Rad50 hook dimerization. (A, top panel) Schematic representation of the Mre11 complex in two possible configurations. Rad50 globular domain shown in brown, Mre11 is in blue, and Nbs1 is in gray. (Bottom panel) Sequence of the hook domain from S. cerevisiae, Mus musculus, and the Rad50⁴⁶ and Rad50⁴⁷ mutants. (B) Gel filtration profile of Rad50-HK proteins. (C) Fractions from B were resolved on an acrylamide gel and stained with Coomassie. (D) Molecular weight and Zn²⁺ content of the indicated Rad50-HK proteins determined by SEC-MALS and ICP-MS, respectively. Theoretical molecular weight for a monomeric (P1), dimeric (P2 and Rad50-HK^WT), and trimeric/tretrameric (P3) species.