Yixin Xu

ORCID: 0000-0003-0014-3899
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About
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Research Areas
  • Advanced Electron Microscopy Techniques and Applications
  • Electron and X-Ray Spectroscopy Techniques
  • Photosynthetic Processes and Mechanisms
  • Microtubule and mitosis dynamics
  • Enzyme Structure and Function
  • Advanced X-ray Imaging Techniques
  • Anodic Oxide Films and Nanostructures
  • Biopolymer Synthesis and Applications
  • DNA Repair Mechanisms
  • Ubiquitin and proteasome pathways

University of Hong Kong
2022-2024

ETH Zurich
2024

Hong Kong University of Science and Technology
2022-2024

Abstract γ-Tubulin ring complex (γ-TuRC) is the major microtubule-nucleating factor. After nucleation, microtubules can be released from γ-TuRC and stabilized by other proteins, such as CAMSAPs, but biochemical cross-talk between minus-end regulation pathways poorly understood. Here we reconstituted this process in vitro using purified components. We found that all CAMSAPs could bind to minus ends of γ-TuRC-attached microtubules. CAMSAP2 CAMSAP3, which decorate stabilize growing not tracking...

10.1038/s41556-024-01366-2 article EN cc-by Nature Cell Biology 2024-02-29

Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from geometry of α-/β-tubulin in microtubule, explaining complex's poor nucleating activity. Several proteins may activate γ-TuRC, mechanisms underlying activation are not known. Here, we determined porcine γ-TuRC purified using CDK5RAP2's centrosomin motif 1 (CM1). We identified an unexpected conformation bound to multiple protein modules containing MZT2, GCP2, and CDK5RAP2, resulting a...

10.1016/j.devcel.2024.09.002 article EN cc-by Developmental Cell 2024-09-01

The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly that provides a template for microtubule nucleation. γ-TuRC recruited to microtubule-organizing centers (MTOCs) by the evolutionarily conserved attachment factor NEDD1. However, structural basis of NEDD1–γ-TuRC interaction not known. Here, we report cryo-EM structures NEDD1 bound human in absence or presence activating CDK5RAP2. We found C-terminus forms tetrameric α-helical contacts lumen cone and orients its...

10.1083/jcb.202410206 article EN cc-by The Journal of Cell Biology 2025-05-21

Recent technological breakthroughs in single-particle cryo-electron microscopy (cryo-EM) enable rapid atomic structure determination of biological macromolecules. A major bottleneck the current single particle cryo-EM pipeline is preparation good quality frozen grids, which mostly a trial-and-error process. Among many issues, preferred orientation and sample damage by air-water interface (AWI) are common practical problems. Here we report method applying metallo-supramolecular branched...

10.1038/s42003-023-05752-8 article EN cc-by Communications Biology 2024-01-09

Abstract Recent technological breakthroughs in single-particle cryo-electron microscopy (cryo-EM) enabled rapid atomic structure determination of biological macromolecules. A major bottleneck the current single particle cryo-EM pipeline is preparation good quality frozen grids, which mostly a trial-and-error process. Among many issues, preferred orientation and sample damage by air-water interface (AWI) are common practical problems. Here we reported method applying metallo-supramolecular...

10.1101/2022.06.08.495397 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-06-09
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