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Figure 2
The bovine bc1 structures determined by cryo-EM. Local resolution maps, coloured on the same scale, of (a) apo bc1, (b) bc1–GSK932121 and (c) bc1–SCR0911, which show that the core of the complex is at the highest resolution and that the Rieske protein is the poorest resolved feature in the map. A comparison of the map quality within each map (coloured grey, gold and cyan for the apo, GSK932121-bound and SCR0911-bound structures, respectively) is shown for two representative transmembrane helices (d, e) and a β-strand within the soluble domain (f). In (d)–(f), the density was contoured at 4σ, with the side chains being better resolved in the two inhibitor-bound structures.

Volume 5| Part 2| March 2018| Pages 200-210
ISSN: 2052-2525