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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | Cryo-EM reconstruction of undecorated GDP microtubule | ||||||||||||
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Sample |
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Keywords | Microtubule. Tubulin dimer. / STRUCTURAL PROTEIN | ||||||||||||
| Function / homology | Function and homology informationstructural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / mitotic cell cycle / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / hydrolase activity / GTPase activity / GTP binding / metal ion binding / cytoplasm Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||||||||
Authors | Munoz-Hernandez H / Wieczorek M | ||||||||||||
| Funding support | Switzerland, 3 items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2026Title: A cryo-EM processing pipeline for microtubules using CryoSPARC. Authors: Daniel Zhang / Hugo Muñoz-Hernández / Pavel Filipcik / Kushal Sejwal / Yixin Xu / Sung Ryul Choi / Michel O Steinmetz / Michal Wieczorek / ![]() Abstract: Microtubules are cytoskeletal filaments that are typically characterized by a discontinuous helical lattice of α/β-tubulin heterodimers. Microtubules can also adopt variable lattice architectures ...Microtubules are cytoskeletal filaments that are typically characterized by a discontinuous helical lattice of α/β-tubulin heterodimers. Microtubules can also adopt variable lattice architectures both in vitro and in cellular contexts. Pseudo-helical averaging processing strategies have been developed to generate cryo-EM reconstructions of microtubules with and without decorating protein-binding partners, but these pipelines can be difficult to implement for the average user, especially for undecorated filaments. Here, we describe MiCSPARC, a cryo-EM processing pipeline developed around CryoSPARC [Punjani et al. (2017), Nat. Methods, 14, 290-296], which leverages automated particle picking and fast 3D refinement times in CryoSPARC to determine the structures of both decorated and undecorated microtubules. We generate reconstructions of undecorated GDP microtubules, as well as kinesin-1 motor domain-decorated GMPCPP filaments, at resolutions of up to 2.8 Å, demonstrating the robustness of the pipeline. Based on its convenient implementation and its ability to routinely generate high-resolution, seam-corrected microtubule reconstructions, MiCSPARC should provide a valuable tool for understanding microtubule dynamics, microtubule-associated proteins and microtubule-targeting agents. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_55431.map.gz | 30.6 MB | EMDB map data format | |
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| Header (meta data) | emd-55431-v30.xml emd-55431.xml | 32 KB 32 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_55431_fsc.xml | 8.4 KB | Display | FSC data file |
| Images | emd_55431.png | 42 KB | ||
| Filedesc metadata | emd-55431.cif.gz | 6.7 KB | ||
| Others | emd_55431_additional_1.map.gz emd_55431_additional_2.map.gz emd_55431_additional_3.map.gz emd_55431_additional_4.map.gz emd_55431_additional_5.map.gz emd_55431_half_map_1.map.gz emd_55431_half_map_2.map.gz | 475.5 MB 59.3 MB 475.5 MB 206.8 MB 20.9 MB 59.3 MB 59.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55431 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55431 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9t1dMC ![]() 9t17C C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_55431.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.067 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Half B Undecorated Microtubule (13-3)
| File | emd_55431_additional_1.map | ||||||||||||
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| Annotation | Half B Undecorated Microtubule (13-3) | ||||||||||||
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-Additional map: Sharpened map
| File | emd_55431_additional_2.map | ||||||||||||
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| Annotation | Sharpened map | ||||||||||||
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-Additional map: Half A Undecorated Microtubule (13-3)
| File | emd_55431_additional_3.map | ||||||||||||
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| Annotation | Half A Undecorated Microtubule (13-3) | ||||||||||||
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-Additional map: Undecorated Microtubule (13-3)
| File | emd_55431_additional_4.map | ||||||||||||
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| Annotation | Undecorated Microtubule (13-3) | ||||||||||||
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-Additional map: #1
| File | emd_55431_additional_5.map | ||||||||||||
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-Half map: #2
| File | emd_55431_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_55431_half_map_2.map | ||||||||||||
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Sample components
-Entire : Undecorated GDP microtubules
| Entire | Name: Undecorated GDP microtubules |
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| Components |
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-Supramolecule #1: Undecorated GDP microtubules
| Supramolecule | Name: Undecorated GDP microtubules / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Detyrosinated tubulin alpha-1A chain
| Macromolecule | Name: Detyrosinated tubulin alpha-1A chain / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 48.784016 KDa |
| Sequence | String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFSVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE ...String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFSVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IYDICRRNLD IERPTYTNLN RLIGQIVSSI TA SLRFDGA LNVDLTEFQT NLVPYPRAHF PLATYAPVIS AEKAYHEQLS VAEITNACFE PANQMVKCDP RHGKYMACCL LYR GDVVPK DVNAAIATIK TKRTIQFVDW CPTGFKVGIN YEPPTVVPGG DLAKVQRAVC MLSNTTAIAE AWARLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV GVDS UniProtKB: Tubulin alpha-1A chain |
-Macromolecule #2: Tubulin beta chain
| Macromolecule | Name: Tubulin beta chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 48.113129 KDa |
| Sequence | String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS ...String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS VHQLVENTDE TYCIDNEALY DICFRTLKLT TPTYGDLNHL VSATMSGVTT CL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVAAVF RGR MSMKEV DEQMLNVQNK NSSYFVEWIP NNVKTAVCDI PPRGLKMSAT FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDAT UniProtKB: Tubulin beta chain |
-Macromolecule #3: GUANOSINE-5'-TRIPHOSPHATE
| Macromolecule | Name: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: GTP |
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| Molecular weight | Theoretical: 523.18 Da |
| Chemical component information | ![]() ChemComp-GTP: |
-Macromolecule #4: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: GUANOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: GDP |
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| Molecular weight | Theoretical: 443.201 Da |
| Chemical component information | ![]() ChemComp-GDP: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 6.8 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 80.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 81000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-9t1d: |
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About Yorodumi




Keywords
Authors
Switzerland, 3 items
Citation







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FIELD EMISSION GUN

