Extended Data Fig. 4: Structural heterogeneity and consensus features of 1:2:1 LDL–LDLR–legobody complexes. | Nature

Extended Data Fig. 4: Structural heterogeneity and consensus features of 1:2:1 LDL–LDLR–legobody complexes.

From: Structure of apolipoprotein B100 bound to the low-density lipoprotein receptor

Extended Data Fig. 4

Reconstructions of each of six subclasses (0–5) includes the particle count, Gold Standard Fourier Shell Correlation Curves for no mask (blue) loose mask (green), tight mask (red), and corrected (purple), inset central section of map with resolution (0.143), Viewing Direction Distribution plot, and orthogonal views with map contour threshold and associated protein structure orientation (top) coloured as in Fig. 3 with apoB100 NTD (blue), LDLR (R, pink), and legobody (L, grey). Unique or missing features are outlined: missing β-barrel and β-propeller (red rectangles), missing legobody (blue rectangle), missing α3 (black ovals), different α2 base (purple rectangle), missing α2 arm (orange rectangles).

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