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Yorodumi- EMDB-16436: microtubule decorated with tubulin oligomers in presence of APC C... -
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Open data
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Basic information
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| Title | microtubule decorated with tubulin oligomers in presence of APC C-terminal domain. (here only map corresponding to the external tubulin oligomer is represented) | |||||||||
Map data | ||||||||||
Sample |
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| Biological species | ![]() | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 36.9 Å | |||||||||
Authors | Serre L / Arnal I | |||||||||
| Funding support | France, 1 items
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Citation | Journal: J.Cell.Sci. / Year: 2022Title: The mitotic role of Adenomatous Polyposis Coli requires its bilateral interaction with tubulin and microtubules Authors: Serre L / Delaroche J / Vinit A / Schoehn G / Denarier E / Fourest-Lieuvin A / Arnal I | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_16436.map.gz | 118.3 MB | EMDB map data format | |
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| Header (meta data) | emd-16436-v30.xml emd-16436.xml | 15.4 KB 15.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_16436_fsc.xml | 14.9 KB | Display | FSC data file |
| Images | emd_16436.png | 48.2 KB | ||
| Others | emd_16436_half_map_1.map.gz emd_16436_half_map_2.map.gz | 98.2 MB 98.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16436 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16436 | HTTPS FTP |
-Validation report
| Summary document | emd_16436_validation.pdf.gz | 640.9 KB | Display | EMDB validaton report |
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| Full document | emd_16436_full_validation.pdf.gz | 640.5 KB | Display | |
| Data in XML | emd_16436_validation.xml.gz | 18.7 KB | Display | |
| Data in CIF | emd_16436_validation.cif.gz | 24.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16436 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16436 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_16436.map.gz / Format: CCP4 / Size: 125 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: 1.96 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_16436_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_16436_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : ring-like tubulin oligomers decorating microtubules.
| Entire | Name: ring-like tubulin oligomers decorating microtubules. |
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| Components |
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-Supramolecule #1: ring-like tubulin oligomers decorating microtubules.
| Supramolecule | Name: ring-like tubulin oligomers decorating microtubules. / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: ALPHA-TUBULIN
| Macromolecule | Name: ALPHA-TUBULIN / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Sequence | String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVR TGTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH S FGGGTGSG FTSLLMERLS VDYGKKSKLE ...String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVR TGTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH S FGGGTGSG FTSLLMERLS VDYGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IY DICRRNL DIERPTYTNL NRLIGQIVSS ITASLRFDGA LNVDLTEFQT NLVPYPRIHF PLATYAPVIS AEK AYHEQL SVAEITNACF EPANQMVKCD PRHGKYMACC LLYRGDVVPK DVNAAIATIK TKRTIQFVDW CPTG FKVGI NYQPPTVVPG GDLAKVQRAV CMLSNTTAIA EAWARLDHKF DLMYAKRAFV HWYVGEGMEE GEFSE ARED MAALEKDYEE VGVDSVEGEG EEEGEEY |
-Macromolecule #2: BETA-TUBULIN
| Macromolecule | Name: BETA-TUBULIN / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Sequence | String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLE PGTMDSVRSG PFGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV V RKESESCD CLQGFQLTHS LGGGTGSGMG TLLISKIREE YPDRIMNTFS ...String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLE PGTMDSVRSG PFGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV V RKESESCD CLQGFQLTHS LGGGTGSGMG TLLISKIREE YPDRIMNTFS VMPSPKVSDT VV EPYNATL SVHQLVENTD ETYCIDNEAL YDICFRTLKL TTPTYGDLNH LVSATMSGVT TCL RFPGQL NADLRKLAVN MVPFPRLHFF MPGFAPLTSR GSQQYRALTV PELTQQMFDS KNMM AACDP RHGRYLTVAA IFRGRMSMKE VDEQMLNVQN KNSSYFVEWI PNNVKTAVCD IPPRG LKMS ATFIGNSTAI QELFKRISEQ FTAMFRRKAF LHWYTGEGMD EMEFTEAESN MNDLVS EYQ QYQDATADEQ GEGHEDEEKD EGG |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 6.7 / Details: 80 mM Pipes, 1 mM MgCl2, 1mM EGTA, 50 mM KCl |
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 303 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
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Authors
France, 1 items
Citation

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Processing
FIELD EMISSION GUN

