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.

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.

The high-resolution structure of Rea1, an essential ribosome maturation factor in Saccharomyces cerevisiae, explains how the ATPase domain is regulated and reveals the linker domain, the mechanical element carrying out ribosome remodeling.

The origin recognition complex is a dynamic complex that assumes various conformational states that likely correspond to different steps in replication initiation.

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.

A fibrillin-related protein, FBN-1, is a key component of the apical extracellular matrix and prevents epidermal cell deformation by biomechanical forces during morphogenesis of the C. elegans embryo.

Integrative structural analyses of human insulin degradingenzyme (IDE) reveal how IDE selectively degrades peptides that form toxicaggregates, which guides IDE-based therapeutic innovations to treat diabetesand Alzheimer's disease.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

A combination of high-resolution structure determination, electrophysiology, and MD simulations reveal fundamental insight into the molecular function of voltage-gated chloride channels.

CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.