First paper: Microtubule doublet in high resolution
- builab
- May 2, 2017
- 1 min read
After 2 years of hard work, we finally published our first paper on the structure of the microtubule doublet at sub-nanometre resolution, the highest to-date for microtubule doublet.
We found that new classes of microtubule-inner proteins, in particular, the filamentous microtubule inner proteins, which bind along the inner ridge of the protofilament pairs.
Link to publication:
https://www.nature.com/articles/ncomms15035
Impressive structural biology breakthrough! Achieving sub-nanometer resolution on microtubule doublets is a massive feat given how complex and polymorphic these structures are. It’s fascinating to see how the discovery of these filamentous microtubule-inner proteins clarifies the arrangement of the lattice and its role in ciliary movement. Great work by the Bui Lab!
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Impressive structural biology breakthrough! Dr. Huy Bui's McGill lab achieved subnanometer-resolution visualization of ciliary doublet microtubules using cryo-electron microscopy—a technically demanding feat given these structures' complexity and polymorphism. The 2017 Nature Communications paper reveals new classes of microtubule-associated proteins and unambiguously assigns α/β-tubulin positions within the doublet lattice, answering fundamental questions about how cilia balance flexibility with structural integrity during bending motion. This work builds on Bui's earlier electron cryo-tomography studies of Chlamydomonas flagella, demonstrating methodological advances in overcoming radiation damage and missing-wedge artifacts through particle averaging. Understanding these molecular arrangements has implications for ciliopathies and cellular motility disorders. Excellent example of cutting-edge structural cell biology emerging from McGill! --bing
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