Structural and functional studies of a potassium ion channel that is opened and closed by different ligands have revealed a novel gating mechanism.

A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.

A combination of direct-electron detectors and statistical movie processing allows ribosome cryo-EM structures to be determined to resolutions that were previously only attainable by X-ray crystallography.

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

Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex

The details of how the enzyme DNA polymerase α initiates the polymerization of nucleotides in DNA replication, a critical step in the synthesis of new chromosomal DNA, have been revealed in atomic detail.

Ubiquitin ligase adaptors target the selective clearance of misfolded plasma membrane proteins.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.