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. 2022 Sep 20;3:e16. doi: 10.1017/qrd.2022.13

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© The Author(s) 2022

This is an Open Access article, distributed under the terms of the Creative Commons Attribution-NoDerivatives licence (http://creativecommons.org/licenses/by-nd/4.0), which permits re-use, distribution, and reproduction in any medium, provided that no alterations are made and the original article is properly cited.

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Fig. 2. — Models obtained from AlphaFold2 and the refinements using Cryo-EM map 12183–7BGL-A-T1047S1D1 (EMDB-PDB-chain ID-CASP14 target ID) and hybrid density maps at 6 and 8 Å resolutions. (a) Superposition of the protein structure (red, chain A of 7BGL) and the model obtained from AlphaFold2 (yellow). This chain is one of the free modelling targets in CASP14 with ID T1047S1D1. (b1) The box-cropped region of cryo-EM map 12183 (EMDB ID, cyan) superimposed with the model (blue) refined using Phenix and the cryo-EM map. (b2) Superposition of the structure (red, chain A of 7BGL) and the refined model (blue) using Phenix and the box-cropped cryo-EM map in b1. Hybrid maps of 6 Å (grey in c1) and 8 Å (yellow in d1) resolutions are superimposed with the model refined from the corresponding map. The 6 Å-map-refined model (Cyan ribbon in c1, c2) and 8 Å-map-refined model (green in d1, d2) are superimposed with the structure (red) in c2 and d2.