Supplementary Figure 12: Tilt angles up to 50° provide near-atomic resolution single-particle reconstructions.
From: Addressing preferred specimen orientation in single-particle cryo-EM through tilting
(a) 3D reconstruction from a preferred oriented LSUbL17dep ribosomal intermediate dataset, where particles were combined from all super-classes but only using data from 50° tilted images. The sample heterogeneity from combining different super-classes is reflected in the local resolution colored onto the reconstruction. Whereas the peripheral density changes, the homogeneous core components are much better resolved. (b) Global half-map 3D FSC and (c) map-to-model 3D FSC. The high tilt angle used for collection results in nearly spherical 3D FSCs, with sphericity of 0.98 and 0.92 respectively. (d) The ten best resolved ribosomal proteins have resolutions of between 4.2 Å and 4.8 Å. (e-g) Map density of (e) bL21, (f) bL20 and (g) uL29 show side chain density and separation of beta strands.
