Browse our latest Structural Biology and Molecular Biophysics articles

SmartScope is the first software package designed to streamline, standardize, and fully automate screening of specimens in cryo-electron microscopy, providing real-time remote control of the microscope and access to data through a standard web interface.

Reconstructed ancestral muscle-type acetylcholine receptor β-subunits readily form homopentameric ion channels that open spontaneously, and display functional hallmarks of the modern-day heteropentameric receptor despite being devoid of canonical agonist-binding sites.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.

Single-particle cryo-EM structures reveal a multistep process of how DNA is loaded into the DNA sliding clamp proliferating cell nuclear antigen by the canonical clamp loader replication factor C.

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

The sour receptor, OTOP1, and related proton channel OTOP3 are steeply activated by extracellular protons while OTOP2 is active over a broad pH range and differences in gating are partly attributed to extracellular domains.

Switches in cell state downstream of pathogen exposure are driven by a deeply conserved disorder-to-order phase transition in an immunity signaling network.

The spider venom peptide Pn3a recognizes a pharmacophore unique to Ca_V3.3 amongst T-type calcium channels, underscoring its potential as a novel molecular tool for the study of Ca_V3.3-mediated currents in native cells.

For analyzing time-dependent patch-clamp or patch-clamp fluorometry data of ion channels in terms of Markovian models, the superiority of Bayesian filtering with respect to traditional deterministic approaches is demonstrated enabling more reliable quantification of the parameters.

The entry glycoproteins of hepatitis C virus, E1E2, possess a novel regulatory mechanism in which protein disorder is harnessed to control their activity and their ability to evade antibodies.