We showed how germline precursors of VRC01-class broadly neutralizing antibodies could bind to HIV envelope by tailoring the protein and glycan moieties.
We determined the first structure of a human antibody in complex with the Epstein-Barr virus glycoproteins revealing an unprecedented mechanism of neutralization of dual-tropic infection.
Our work provides a structural framework to understand how enterotropic coronaviruses evolved to fine-tune fusion activation in the protease-rich environment of the small intestine.
We characterized a cyclic nucleotide-gated ion channel using cryoEM to yield new insights about the mode of action of this medically important channel family.
The cryoEM reconstruction of the proteasome at 2.8 Å resolution enables identifying amino-acid side chains rotamers and resolving ordered water molecules.