Supplementary Figure 3: Cryo-EM structure of the reconstituted 40S–ABCE1 complex and assessment of resolution.
From: Structure of the 40S–ABCE1 post-splitting complex in ribosome recycling and translation initiation
a, Cryo-EM density of the 40S–ABCE1 complex and isolated ABCE1 low-pass filtered at 3.9 Å showing the 40S subunit (grey), and ABCE1 (red), as well as local resolution as calculated by ResMap. The ResMap plots show a range from maximum 3.5 Å to 8.5 Å in the periphery. It is to note, in ABCE1, the FeS cluster domain and NBD1 are well resolved whereas resolution in NBD2 and peripheral regions of ABCE1 is slightly decreased. Maps are contoured at 3.5 σ. b, FSC plot shows the 3.9 Å average resolution of the map according to the “gold standard” criterion (FSC = 0.143; top) and FSC curves calculated between the cryo‑EM map and the final models (bottom) as calculated by REFMAC. Values are plotted for the model versus the final map (FSCaverage, black), for the model that was refined into the first half-map and FSC calculated either for the same map (model vs first half-map, orange) or for the second half-map (model vs second half map, blue). c, Density snapshots of isolated ABCE1 (contoured as indicated in the panels) with the fitted model shown in three orientations. Below, selected areas are shown illustrating the quality of the map (side chain densities in the α-helices forming the HLH motif; a separated β-sheet in NBD1 and a β-sheet with resolved bulky side chains in hinge 2). Domains are colored as indicated in the schematic panel.
