X-ray and cryo-EM structures of inhibitor-bound cytochrome bc1 complexes for structure-based drug discovery

Amporndanai, K.; Johnson, R.M.; O'Neill, P.M.; Fishwick, C.W.G.; Jamson, A.H.; Rawson, S.; Muench, S.P.; Hasnain, S.S.; Antonyuk, S.V.

doi:10.1107/S2052252518001616

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.

IUCrJ

Volume 5| Part 2| March 2018| Pages 200-210

ISSN: 2052-2525

https://doi.org/10.1107/S2052252518001616

CRYO | EM

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