I. I. Serysheva

The paper determines 3D structures of IP3R1 in two ligand-bound states using cryo-EM and identifies dynamic properties of key domains involved in ligand binding and channel gating.

This study identifies acidic residues in IP3Rs critical for Ca2+ binding and activation, showing their role in modulating channel activity and Ca2+ sensitivity.

The paper uses cryo-ET to determine the 7 Å structure of the AcrAB-TolC efflux pump in Escherichia coli, revealing its activation mechanism through interprotein interactions.

The paper presents cryo-EM structures of InsP3R1 in activated and apo-states, revealing ligand-induced conformational changes that underlie channel gating.