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.

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.

Combining cerebral organoid technology with cryo-correlative microscopy reveals the organization of cytoskeleton, membrane compartments, and protein synthesis machinery contributing to the rapid expansion of developing human axons.

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.

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.

The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.

A freely available software environment on Amazon's cloud computing network makes processing of cryo-EM data accessible and affordable.

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.

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.

CryoEM structures of open gyrase A dimers and DNA in two states representing steps either prior to or after passage through the DNA-gate, show where a putative T-segment is found.