High-resolution optical microscopy is used to reveal the organization of extracellular matrix proteins within the basement membrane of the blood filtration barrier in the kidney at the nanometer scale.

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

Biochemical and genetic approaches revealed a posttranslational mechanism controlling the abundance of SUN2, a critical nuclear envelope protein.

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

A combination of light and electron microscopy data provide new insights into the dynamic architecture and the function of the endocytic protein machinery in relation to membrane shape changes in vivo.

Cryo-electron tomography of close-to-native rod outer segments resolves connectors between disks and a scaffold at the disk rim enforcing the high membrane curvature of the unique long-range organization in these rhodopsin-rich light-sensitive subcellular organelles.

Loss of the transcription factor Rreb1 results perturbs epithelial architecture during mouse development resulting in invasive cell behaviors, severe cardiovascular defects, and embryonic lethality.

Uniform diameter and curvature of the outer membrane extensions and vesicles of Shewanella oneidensis are maintained by a bacterial Bin/Amphiphysin/Rvs (BAR) domain-like protein BdpA.

The axial organization and dynamics of the HOPS complex at membrane surface are resolved by graphene-induced energy transfer with subnanometer resolution.