Cryo-EM studies of doublet microtubules from wild-type and acetylation mutants suggest that acetylation of K40 affects the lateral rotational angle between protofilaments, leading to changes in the structure and stability.

A structure of the ciliary inner junction at 3.6 Å resolution permits atomic modeling of six inner junction proteins and their interactions with acetylated lysine 40 loops of alpha tubulins.

Zebrafish genetics and sperm cryo-electron tomography reveal a novel function of Calaxin as a docking complex component stabilizing the outer arm dynein onto the ciliary doublet microtubule.

Cryo-electron tomography of mammalian and fly centrioles shows that the ninefold symmetry of centrioles is set by species-specific microtubule linkers.

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.

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.

CCDC146 is a structural component of the flagellum in sperm, located in the doublet microtubules of the axoneme, whose absence leads to multiple morphological anomalies of the flagellum.

Relion was used to solve structures of microtubules decorated with dynein microtubule-binding domains revealing that an axonemal dynein distorts the microtubule cross-sectional curvature.

Cryo-electron microscopy reveals previously undescribed structural features of choanoflagellate flagella and provides new insights into flagellar evolution.

The structural and functional analysis demonstrates the mechanism of dual functional, motility and microtubule depolymerization in a unique motor, KIF19A.