Supplementary Figure 2: Resolution of the 60S-ribosomal-subunit complexes and validation of the atomic model.
From: Mechanism of eIF6 release from the nascent 60S ribosomal subunit
(a) Gold-standard Fourier shell correlation (FSC) curves for the three 60S ribosome complexes after 3D refinement and statistical movie processing in RELION (Bai, X. C. et al., Elife 2, e00461, 2013; Scheres, S. H. J Struct Biol 180, 519-530, 2012).
(b) Surface (top panel) and cross-sectional (bottom panel) views of the unsharpened final maps colored according to local resolution calculated with the ResMap software package (Kucukelbir, A. et al., Nat Methods, 11, 63-65, 2014).
(c, d, e, f) Examples of densities with the model fitted showing helix 72 of the 26S rRNA from the 60S-eIF6-SBDS complex with the density filtered at 3.3 Å (c), α-helix of the uL6 protein from the 60S-eIF6-SBDS complex with the density filtered at 3.3 Å (d), SBDS from the 60S-eIF6-SBDS complex with the density is filtered at 4 Å (e), EFL1 from the 60S-eIF6-SBDS-EFL1 complex with the density is filtered at 8 Å (f).
(g, h, i) Cross-validation against over-fitting. FSC curves are shown for the 60S-eIF6-SBDS (g), 60S-eIF6-SBDS-EFL1 (h) and 60S-SBDS-EFL1 (i) complexes between the final refined atomic model and the reconstructions from all particles (black); between the model refined in the reconstruction from only half of the particles and the reconstruction from that same half (FSCwork, red); and between that same model and the reconstruction from the other half of the particles (FSCtest, green).
