Super-resolution microscopy reveals, at nanometric-scale, the highly organized protein structure of viroplasms, the viral factories used by rotavirus to replicate its genome and assemble new viral particles.

Super-resolution microscopy sets a new strategy to comprehend the membrane organization of γ-secretase at single complex resolution identifying nanodomain associations and its diffusion in situ in the living membrane.

Building on previous work (Grotjohann et al., 2012), low-light super-resolution microscopy has been performed on living transgenic Drosophila larvae and tissues.

Super-resolved architectural framework of subdistal appendages surprisingly reveals coupling between distal appendages and subdistal appendages.

Super-resolution microscopy reveals the nanoscale molecular architecture of 29 protein components of a eukaryotic contractile ring relative to the membrane.

Machine learning in conjunction with super-resolution imaging allows for the first time to quantitatively analyse large and heterogenous virus samples structure at a high throughput and specificity.

Clustering the B cell receptor generates a membrane domain analogous to the liquid-ordered phase, localizing proteins involved in early receptor activation.

Quantitative super-resolution light microscopy reveals the relative abundance and three-dimensional organization of different microtubule subsets within dendrites of mammalian neurons.

The two Drosophila titin homologs Sallimus and Projectin display a precise tandem arrangement in the sarcomere that may explain how sarcomere length is regulated outside of vertebrates.

Neuroligin 1 is a critical adhesion molecule which organizes AMPA receptor nanodomains in close vicinity to pre-synaptic release sites, and whose genetic or chemical disruption severely impairs synaptic transmission properties.