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![[Figure 2]](ir5011fig2mag.jpg)
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Figure 2
Low-resolution (3.1 Å) apoferritin maps. (a) Original 3.1 Å resolution apoferritin map, half-map sharpened (Terwilliger et al., 2018  ). (b) Map obtained using density modification but no model-based information. (c) Map obtained using an automatically generated ensemble model. The model shown is from the crystallographic structure of human apoferritin (Masuda et al., 2010), re-refined against the 1.8 Å resolution apoferritin map (EMDB EMD-20026). Arrows indicate locations in the map where the clarity is improved by density modification. (d) Fourier shell correlation of the maps shown in (a) (blue; labeled initial map), (b) (orange; labeled density modified) and (c) (black; labeled density modified with models) with the high-resolution (1.8 Å) apoferritin map (EMDB EMD-20026). The density-modification analysis was carried out to a resolution of 2 Å so all Fourier terms from the density-modified map are zero beyond this resolution and therefore all FSC values are zero as well. |
![[Figure 2]](ir5011fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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