Extended Data Fig. 4: Structural features of our cryo-EM maps at 1.55/1.25 Å resolution compared to the thus far reported highest-resolution map at 1.54 Å resolution (EMDB-9865). | Nature

Extended Data Fig. 4: Structural features of our cryo-EM maps at 1.55/1.25 Å resolution compared to the thus far reported highest-resolution map at 1.54 Å resolution (EMDB-9865).

From: Atomic-resolution protein structure determination by cryo-EM

Extended Data Fig. 4

Three apoferritin residues (His151, Phe51, Arg76) are shown at two different density thresholds in three cryo-EM maps. Row one depicts our present high-resolution map at 1.25 Å; resolution and row three shows a structure at 1.55 Å; resolution obtained from a smaller subset of the same data. Only 22.000 particles were necessary for this reconstruction to obtain 1.55 Å resolution which is a 5.5× lower particle statistics compared to the 1.54 Å Jeol CryoARM300 map (second row). The low-threshold density meshes are always shown in grey and H atoms (white sticks) are included in the corresponding atomic models. Only in the Krios Mono/BCOR structure at 1.25 Å; resolution density becomes visible to accommodate all hydrogen atoms. At higher thresholds the two structures at 1.54 Å and 1.55 Å resolution nicely maintain the shapes of the sidechains but only in the structure at 1.25 Å; resolution individual atoms become clearly separated from each other indicating true atomic resolution.

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