Fig. 3: Benchmarking performance of TomoBEAR. | Nature Communications

Fig. 3: Benchmarking performance of TomoBEAR.

From: Streamlined structure determination by cryo-electron tomography and subtomogram averaging using TomoBEAR

Fig. 3

a Processing of the tomographic data sets of purified ribosomes (EMPIAR 10064, mixed defocus): A structure at resolution 11.0 Å sliced in the middle of the reconstruction and colored according to local resolution. Black scale bars: 10 nm. Lower panels: detection of resolution based on Fourier Shell Correlation between independently refined half-sets. b Structure of purified human apoferritin imaged by cryo-ET in this study at the global resolution of 2.8 Å. The map is sliced in the middle of the reconstruction and colored according to local resolution. c Processing of tomograms of an ion channel RyR1 imaged in native membranes purified from rabbit muscle (EMPIAR-10452). The structure of RyR1 at a resolution of 8.9 Å sliced in the middle of the reconstruction and colored according to local resolution. Estimation of resolution based on Fourier Shell Correlation: the curves for the original processing of this data set from ref. 37 are in orange and blue, magenta - from TomoBEAR+RELION4.

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