The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.

The structure of the potassium-chloride cotransporter KCC4 provides insight into the basis of ion specificity, transport stoichiometry, and activity regulation for a broadly physiologically and clinically important transporter family.

A cryo-EM structure of the SARS-CoV-2 M protein, the most abundant protein in the viral envelope, provides insight into its essential role in virus assembly.

cryo-EM reveals the properties of distinct conformations occupied during activation of the lipid scramblase nhTMEM16 and provides new insights into its interactions with the lipid environment.

The basis for small-molecule block, insights into gating, and an unexpected architectural role for the lipid membrane are revealed in structures of the volume regulated anion channel LRRC8A.

Structures of a TMEM16 phospholipid scramblase reveal that its Ca²⁺-dependent activation entails global conformational changes and how these rearrangements affect the membrane to enable transbilayer lipid transfer.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.

As the function of membrane proteins is often influenced by its membrane environment the presented combinatorial approach is of great value for the investigation of membrane protein complexes in natural or even manipulated lipid bilayers.

While activated by a common mechanism, both functions in TMEM16F - lipid scrambling and ion conduction - are likely mediated by alternate protein conformations that are at equilibrium in the ligand-bound state.

Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.