Cryo electron tomography provides the first high-resolution 3D axoneme structure from any pathogenic organism, revealing novel structures that support the unique motility of these pathogens through host tissues.
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.
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 nature of the phycobilisome–photosystem II supercomplex on the native thylakoid determined with cryo-electron tomography at an unprecedented resolution reveals that one phycobilisome interconnects with six photosystem monomers.
Zebrafish genetics and cryo-electron tomography reveal distinct roles of all vertebrate PIH family proteins in axonemal dynein assembly and cilia/flagella motions, assigning specific dynein subtypes to each PIH protein.
In situ cryo-electron tomography unveils the molecular sociology of a developing sporangium in Bacillus subtilis, revealing critical information about cell wall remodeling and membrane migration in bacteria.
Specific attachment of molecularly defined gold nanoparticles enables precise localization, critical for structural studies in vivo, of proteins of unknown structure within the cellular milieu by cryo-electron tomography.