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. 2020 Jun 10;7(Pt 4):681–692. doi: 10.1107/S2052252520005916

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© Martin Malý et al. 2020

This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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Paired refinement results for models from different building stages: EP (a)–(d) and POLI (e)–(f) data sets. For each incremental step of resolution for X→Y, the R values were calculated at resolution X. EP: resolution shells with a width of 0.05 Å. (a) Model after molecular replacement using a penicillopepsin structure. (b) Protein model as built by ARP/wARP. (c) Original model of endothiapepsin without solvent molecules (PDB entry 4y4g). (d) Structure of endothiapepsin as deposited in the PDB. (e)–(f) POLI: resolution shells with a width of 0.10 Å. (e) Poly-Ala model built by SHELXE into the experimental map. (f) Complete protein model without solvent molecules.