eMags is an engineered photodimerizer pair for optogenetic modulation in mammalian cells that is especially suited for the manipulation of intracellular processes occurring in small volumes or subcellular organelles.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

The genome of Thermovibrio ammonificans encodes ancestral pathways (e.g., hydrogen oxidation) and more recently acquired ones (e.g., nitrate reduction) and a hybrid pathway for CO₂ fixation.

The model organism Tetrahymena thermopile carries two nuclei with distinct genomes: an unrearranged germline genome with five chromosomes, and a somatic genome reduced in size by a third and with 181 chromosomes.

Pulsed-labeling hydrogen exchange on the ribonuclease H family show that the major folding intermediate is conserved over three billion years of evolution, but the path leading to this intermediate varies.

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.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.