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.

By measuring the impacts of thousands of mutations on potassium channel trafficking and function, we illuminate the molecular basis of folding, structure–function relationships, and how these are altered in disease.

The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.

Cryo electron microscopy and structure-based mutagenesis reveal that the bacteriophage BPP-1 contains two of the three major recognized viral folds, one of which exhibits a new topology.

Profiling spatially defined fibroblasts in the pancreatic ductal adenocarcinoma (PDAC) tumor microenvironment identifies high levels of podoplanin and hypoxia in tumor-proximal fibroblasts associated with bad prognosis, whilst inflammatory markers define more distal fibroblast regions and associate with better outcomes.

Sequencing mRNA from thousands of single cells from the Drosophila brain highlights the extent of cellular diversity and reveals co-expression of specific neuropeptides with particular fast-acting neurotransmitters and monoamines.

An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.

Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

A detailed description of the structure of procentriole MT triplet by cryoET, along with its associated non-tubulin proteins and its assembly intermediates, reveals possible molecular mechanism for the procentriole assembly.