The first independent publication from the Berndsen lab @Mizzou_Biochem in collaboration with my colleague @CKeithCassidy is now peer reviewed and online at @Nature !! rdcu.be/d3kfg Resolving a many decades-old challenge, we determined the complete structure of apolipoprotein B100 on the surface of its native #LDL particle using a combination single-particle #cryoEM, #AlphaFold2, and molecular dynamics refinement methods. At ~550 kDa, with ~4.6k residues of mostly extended amphipathic domains, #ApoB is one of the largest and most complex proteins in the genome. Our structure provides insight into lipoprotein synthesis, the structural changes involved in the catabolic conversion from VLDL to LDL, and the nature of disease causing mutations involved in diseases such as #FamilialHypercholesterolemia. The main change from the preprint is the addition of extensive chemical crosslinking data, which validate many of the lower-resolution contacts we observed between the C-terminal inserts and lends support to our proposed model for conformational changes on larger LP particles. With the structure of apoB finally revealed, a new era in lipoprotein research begins were highly precise and targeted structural, genetic, and computational studies are now possible! We have many plans and are excited for what the future of this field holds, so stayed tuned!!