Extended Data Fig. 7: Cross-linking mass spectrometry.
From: Structure of apolipoprotein B100 bound to the low-density lipoprotein receptor
Sulfo-SDA cross-links with Cα-Cα distances ≤ 25 Å (black solid lines) and > 25 Å (black dashed lines) mapped on ribbon diagrams coloured as in Fig. 3 with features of interest as labelled. a, Intramolecular apoB100 cross-links in apoB100 with insets showing long-range cross-links and four clusters of overlength cross-links demonstrating flexibility in βα1 region. b–d, Intermolecular cross-links across the BS2 interface (b), BS1 interface (c) and LA5 module of LDLR to the apoB100 β-barrel (flexible modules of LDLR pink dashed lines) (d). e, Sulfo-SDA cross-links (black dashed lines) mapped on a ribbon diagram coloured as in Fig. 5 across the apoB100 dimer interface. Electron density map of 2:2:2 LDL–LDLR–legobody (transparent grey surface) included for context.
