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Cryo-electron microscopy reveals how kinesin-binding protein inhibits microtubule attachment in a subset of kinesins.

Four αβ-tubulin dimers associate laterally on γ-TuRC to define the rate-limiting transition state for microtubule nucleation.

The corkscrew-like motility of Spirochete bacteria is enabled by a unique, asymmetrically constructed flagellum that wraps around the cell body within the periplasm.

The tubulin GTPase cycle structurally modulates the microtubule cap, causing lattice expansion, which is an intermediate state involved in phosphate release and regulatory signaling.

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.

Two new polymorphic structures of recombinant human alpha-synuclein fibrils show striking differences to previous structures, while familial PD mutation sites remain crucial for protofilament interaction and fibril stability.

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.

A sequential reaction pathway involving TPX2, augmin and γ-TuRC governs the assembly and architecture of branched microtubule networks.

Principal curvature-dependent motion of bacterial actin MreB results in localization consistent with all known literature.

C. elegans EFHC1 influences neuronal transmission through the cilium and the synapse.