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![[Figure 3]](ir5011fig3mag.jpg)
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Figure 3
Control analysis using model density based on incorrect side-chain conformations. (a)–(f) are analyses varying the target density for Phe81 and (g)–(j) are analyses varying the target density for residues Gln14, Arg22, Gln83 and Glu140. (a) High-resolution (1.8 Å) apoferritin map (EMDB EMD-20026), density-modified without model information. A crystal structure of human apoferritin, docked into and partially refined against the EMD-20026 map, but still containing multiple conformations of several side chains is shown. (b) Low-resolution (3.1 Å) apoferritin map (EMDB EMD-20028), density-modified without model information. (c) Target density using conformation A of Phe81. (d) Target density using conformation B of Phe81. (e) Density-modified 3.1 Å resolution apoferritin map including target density from conformation A shown in (c). (f) Density-modified 3.1 Å resolution apoferritin map including target density from conformation B shown in (d). (g)–(j) each show three maps focused on a selected residue: Gln14 in (g), Arg22 in (h), Gln83 in (i) and Glu140 in (j). The maps on the left and middle in each case are density-modified 3.1 Å resolution apoferritin maps including target density from conformation A or B of the selected residue, respectively. The map on the right is the corresponding high-resolution (1.8 Å) density-modified apoferritin map. The A and B side-chain conformations are indicated. Contours for members of each pair of density-modified maps are set at identical levels. |
![[Figure 3]](ir5011fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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