Extended Data Fig. 3: The Cryo-EM structural determination process for the UBC4 complex. | Nature

Extended Data Fig. 3: The Cryo-EM structural determination process for the UBC4 complex.

From: A unified mechanism for intron and exon definition and back-splicing

Extended Data Fig. 3

a, Representative drift-corrected cryo-EM micrograph (out of 8,997 micrographs) of the E complex assembled on the UBC4 pre-mRNA. A representative particle is shown in a white dotted circle. b, Representative 2D class averages of the UBC4 complex obtained in RELION. c, Data processing workflow. For processing above the red dashed line, the particle images were binned to a pixel size of 2.72 Å. The rest of the processing was performed with a pixel size of 1.36 Å. The masks used in data processing are outlined with red solid lines (see Methods). d, Angular distribution of all particles used for the final 3.6 Å map of the UBC4 complex. e, FSC as a function of spatial frequency demonstrating the resolution of the final reconstruction of the UBC4 complex. f, Resmap local resolution estimation. g, FSC coefficients as a functional of spatial frequency between model and cryo-EM density maps. The generally similar appearances between the FSC curves obtained with half maps with (red) and without (blue) model refinement indicate that the refinement of the atomic coordinates did not suffer from severe over-fitting.

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