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 the molecular mechanism of human αVβ3 integrin inhibition by the candidate therapeutic antibody LM609.
First cryoEM structure of a viral fusion protein in the postfusion conformation providing new insights about coronavirus infection.
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.
We identified and characterized type VI secretion system effectors promoting Francisella growth in macrophages.
Our atomic resolution structure of a human coronavirus spike protein highlights strategies used by these viruses to evade the immune system.
We used cryoEM to determine the first structure of a coronavirus spike glycoprotein at near-atomic resolution.
The cryoEM reconstruction of the proteasome at 2.8 Å resolution enables identifying amino-acid side chains rotamers and resolving ordered water molecules.