Electron microscopy has been used to produce the first three-dimensional image of the PRC2 gene-silencing complex.

Histones bound to lipid droplets inside cells offer protection against bacteria in flies, and possibly mice, thus suggesting a possible new innate immunity pathway.

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.

Long-lived intermediate states formed by glycoprotein catalysts are an essential part of the process used by influenza virus particles to infect cells.

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

A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.

Mutagenesis studies identified an androgen receptor mutation that converts enzalutamide-a drug recently approved for the treatment of advanced prostate cancer-into an androgen receptor agonist, and modeling studies informed the design of novel drugs that are effective against the mutant receptor.

Sites at which mitochondria contact the endoplasmic reticulum co-localize the replication of mitochondria and their DNA to help ensure that DNA is distributed appropriately between the newly formed organelles in cells.

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.