Extended Data Fig. 2: Quality of the apo BCDX2 complex cryo-EM reconstruction. | Nature

Extended Data Fig. 2: Quality of the apo BCDX2 complex cryo-EM reconstruction.

From: Structural insights into BCDX2 complex function in homologous recombination

Extended Data Fig. 2: Quality of the apo BCDX2 complex cryo-EM reconstruction.

a, The final Euler angle distribution of particles used for 3D refinement. b, Fourier Shell Correlation (FSC) plot from two half maps, with an overall resolution of 2.3 Å as determined at 0.143 criterion. c, Local resolution map color-coded from lower (red) to higher resolution (blue). d, Overall map (left) and detailed views of local cryo-EM density for selected regions of the BCDX2 complex (right). e, Cryo-EM map of the BCDX2 complex with two views related by a 180° rotation about the y-axis (left). Maps of the individual subunits are shown to the right with RAD51B (pink), RAD51C (green), RAD51D (yellow), XRCC2 (purple).

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