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. 2017 Mar 28;68(14):3857–3867. doi: 10.1093/jxb/erx070

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© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 2. — Gating residues Glu69 and Arg70 in open and closed conformations in the two monomers of SeCcmP_P2₁3. (A) Superposition of the two monomers of SeCcmP_P2₁3. Monomer A (magenta) in an open conformation and monomer B (rainbow coloured) in a closed conformation. The electron density of the ligand extends from the binding pocket of monomer B toward the carbonyl oxygen of Gln66. (B) Well-defined electron density for the gating residues in the closed conformation (monomer B). (C) Electron density for the gating residues in the open conformation (monomer A). (D) The closed end of the pore seen down the three-fold symmetry axis. (E) The open end of the pore seen down the three-fold symmetry axis. Electron densities are from 2F_o–F_c maps contoured at the 1 σ level.