The structure and composition of the elusive vertex complex in Tectiviridae is finally revealed and the newly reported protein conformations help to maintain the capsid architecture.

Mitochondrial anti-viral signaling proteins form three-stranded helical filaments in launching innate immune responses against RNA viruses.

Water molecules and amino-acid side chain rotamers have been resolved in the cryoEM structure of T20S proteasome at 2.8 angstroms.

Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.

Multiple dynamic protein interactions converge to regulate the catalytic activity of the B cell kinase, BTK.

A comprehensive structural analysis of inhibitory murine antibody 3D11 binding to Plasmodium berghei circumsporozoite protein reveals common mechanisms of antibody evolution in mammals against Plasmodium parasites.

The human Origin Replication Complex is shaped as a shallow corkscrew in a classic AAA+ organization reminiscent of clamp loader complexes with highly controlled ATPase activity as exemplified by Meier-Gorlin syndrome mutations.

Cryogenic super-resolution microscopy resolves the three-dimensional arrangement of individual fluorescent markers attached to protein complexes with Angstrom precision through their blinking behavior, polarization selection and a classification scheme.

An integrated cryoEM and X-ray crystallography study resolves the structural basis for antibody-mediated targeting of the hantavirus fusion glycoprotein and provides insight into the conformational landscape of the hantavirion surface.