The structure of a large enzyme complex involved in methanogenesis was determined at high resolution by electron cryo-microscopy.

The structure of a large hydrogenase complex involved in the production of methane by microbes has been determined with cryo-electron microscopy.

Cryo-electron microscopy reveals the structure of a chloride channel that is closely related to a protein that transports lipids.

Cryo-electron microscopy and genetics show how Staphylococcus aureus pathogenicity island 1 hijacks the assembly pathway of a helper phage for its own propagation.

Cryo-electron microscopy structures show how coliphage HK022 Nun blocks Escherichia coli RNA polymerase translocation by mediating multiple interactions between the RNA polymerase and nucleic acids.

Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.

Cryo-electron microscopy structures show how the clinically used antimicrobial fidaxomicin binds and inhibits Mycobacterium tuberculosis RNA polymerase by acting like a doorstop to jam the enzyme in an open conformation via the general transcription factor RbpA.

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.

Structural insights into the architecture and functional properties of zebrafish TRPC4 are revealed by high-resolution cryo-EM.