Extended Data Fig. 6: Heterogeneity of the cholesteryl ester core does not disrupt LDLR binding and the resolution of glycans.

a, Asymmetric single-particle reconstruction of 2:2:2 LDL–LDLR–legobody complexes with matched (blue box), mismatched (yellow box), and disordered (green box) CE plates. Direction of CE plates in each LDL (double-ended arrows) is unchanged in the upper LDL and variable in the lower LDL of each dimer in the uncapped central slices of each reconstruction (right), except where disordered (x). b, Superposition of asymmetric dimer maps with matched (blue), mismatched (transparent yellow), and disordered (green) CE plates and labelled with features of interest. The CE plates are unchanged in the LDL (Same LDL) on the left and variable in the LDL (Different LDL) on the right. Each reconstruction includes density for two LDLR. Far from LDLR, the β-belt of apoB100 adopts different positions coincident with the matched (blue) and disordered (green) CE plates. c–e, N-acetylglucosamine (NAG) are labelled with residue numbers for each. (c) 3.73 Å map near nanobody (grey surface), at density threshold 0.1, with structure (sticks) coloured by heteroatom of glycosylated (grey) N3101 in apoB100 (yellow). d,e, The 1:2:1 complex map (5.41 Å) at density threshold 0.05 (yellow surface) and 0.1 (blue mesh), with glycans (blue sticks and by heteroatom) in the NTD (d) and β-belt (e) of apoB100 (ribbon diagram with side chains labelled, coloured as in Fig. 3 and by heteroatom).