A New Protocol to Accurately Determine Microtubule Lattice Seam Location
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Summary
A new data processing protocol is developed that can accurately determine αβ-tubulin register and seam location for MT segments and visualize the nucleotide state at the E-site and the configuration of lateral contacts at the seam.
- Type
- article
- Published
- 2015-09-28
- Cited by
- 84
- References
- 44
- Access
- Open access
- OpenAlex
- https://openalex.org/W1789623687
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:32929591
Keywords
Tubulin, Microtubule, Cryo-electron microscopy, Lattice (music), Computer science
References
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- Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins
- 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
- Arrangement of subunits in flagellar microtubules.
- Dynamic instability of microtubule growth
- Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy.
- Determination of microtubule polarity by cryo-electron microscopy.
- Tracking the ends: a dynamic protein network controls the fate of microtubule tips
- Movies of ice-embedded particles enhance resolution in electron cryo-microscopy
- Control of the Structural Stability of the Tubulin Dimer by One High Affinity Bound Magnesium Ion at Nucleotide N-site*
- Tubulin and FtsZ form a distinct family of GTPases
- EMAN: semiautomated software for high-resolution single-particle reconstructions.
- Diffraction by Helical Structures with Seams: Microtubules
- EBs Recognize a Nucleotide-Dependent Structural Cap at Growing Microtubule Ends
- High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus.
- FREALIGN: high-resolution refinement of single particle structures.
- A new theory and algorithm for reconstructing helical structures with a seam.
- Refined structure of alpha beta-tubulin at 3.5 A resolution.
Cited by
- Visualizing Microtubule Structural Transitions and Interactions with Associated Proteins
- Near-atomic cryo-EM structure of PRC1 bound to the microtubule
- Resolution advances in cryo-EM enable application to drug discovery
- Modulation of the Polymerization Kinetics of α/β-Tubulin by Osmolytes and Macromolecular Crowding.
- Chirality of the cytoskeleton in the origins of cellular asymmetry
- Characterization of Tau and Anticancer Drug Interactions with Microtubules via Cryo-Electron Microscopy Studies
- Cryo-EM structures of human recombinase RAD51 filaments in the catalysis of DNA strand exchange
- Insights into the distinct mechanisms of action of taxane and non-taxane microtubule stabilizers from cryo-EM structures
- Structural Insights of WHAMM's Interaction with Microtubules by Cryo-EM.
- Triazolopyrimidines Are Microtubule-Stabilizing Agents that Bind the Vinca Inhibitor Site of Tubulin.
- Structural differences between yeast and mammalian microtubules revealed by cryo-EM
- Challenges and opportunities in the high-resolution cryo-EM visualization of microtubules and their binding partners
- A structural model of flagellar filament switching across multiple bacterial species
- Structural insight into TPX2-stimulated microtubule assembly
- Structural and functional differences between porcine brain and budding yeast microtubules
- Determining the RAD51-DNA Nucleoprotein Filament Structure and Function by Cryo-Electron Microscopy.
- Atomic model of microtubule-bound tau
- Near-atomic model of microtubule-tau interactions
- Separating the effects of nucleotide and EB binding on microtubule structure
- Single particle cryo-EM-an optimal tool to study cytoskeletal proteins.
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