T. Legal

DomainFit identifies protein domains in low-resolution cryo-EM maps using AlphaFold2 models, revealing new proteins in cellular complexes.

This study examines how alpha-tubulin acetylation affects doublet microtubule structure in Tetrahymena cilia using cryo-EM, MD, and mass spectrometry, finding small-scale structural changes and a link to phosphorylation.

The paper uses cryo-EM and integrative modeling to localize DRC subunits in the N-DRC of Tetrahymena thermophila and identifies interacting coiled-coil proteins.

This study identifies a BubR1-independent, dynein-dependent pathway for CENP-E recruitment to the outer kinetochore corona and shows its role in assembling the corona with RZZ complex and Mad1.

This study identifies how phosphorylation regulates motor-PRC1 complexes to coordinate chromosome segregation and cytokinesis during mitosis.

The paper uses cryo-electron tomography to reveal the molecular architecture of the ciliary tip in Tetrahymena thermophila, showing cross-linked microtubules and structural features of the central pair.

The paper uses cryo-EM to analyze native doublet microtubules in Tetrahymena thermophila, identifying MIPs and showing their role in cilia function through CFAP77 knockout.

This study reconstitutes active human CENP-E motor and shows that full-length CENP-E has increased processivity and reduced microtubule landing rate compared to truncations.

This study identifies the molecular interaction between BubR1 and CENP-E required for CENP-E recruitment to kinetochores and chromosome alignment during mitosis.