Light and X-ray scattering on the same primate and human brain samples cross-validate each other and enable accurate mapping of axonal trajectories in regions with uni- and multi-directional nerve fibers, which can be used to validate diffusion MRI.

The interaction of SecA with its substrate proteins is regulated by its evolutionarily conserved C-terminal tail, which autoinhibits SecA unless SecA binds to the ribosome.

Self-association of speckle-type POZ protein (SPOP), a substrate adaptor in the ubiquitin proteasome system, is studied by combining small-angle X-ray scattering and molecular dynamics simulations to reveal the structure of the protein assemblies in solution.

The damage of the bacterial cell envelope is found to be only a secondary effect of the antimicrobial activity of lactoferricin derivatives.

The full-length structures of the mammalian nitric oxide receptor reveal the molecular activation steps and a binding site for the prototype of FDA-approved stimulators.

Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.

Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.

A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.

Building on previous work (Chatterjee et al., 2014), the mechanism of coincidence detection in bacterial second messenger signaling across membranes is revealed at a molecular level, providing insight into the regulation of a conserved transmembrane receptor.

A conserved viral protein complex that promotes membrane wrapping of nascent herpesvirus particles shows structural similarity to cellular membrane-remodelling proteins, suggesting functional mimicry.