|Entry||Database: EMDB / ID: 1787|
|Title||Asymmetric reconstruction of doublecortin-stabilised microtubules decorated with kinesin motor domain|
|Keywords||Tubulin / MAP / microtubule / stabilisation / doublecortin / kinesin|
|Sample||Microtubules co-polymerised with doublecortin and bound with kinesin motor domain|
|Source||Bos taurus / mammal / Bovine / ウシ / |
Homo sapiens / human
Rattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /
|Map data||This is a C1 reconstruction of doublecortin-stabilised microtubule decorated with kinesin motor domain|
|Method||single particle reconstruction, at 13.5 Å resolution|
|Authors||Fourniol FJ / Sindelar CV / Amigues B / Clare D / Thomas G / Perderiset M / Francis F / Houdusse A / Moores CA|
|Citation||J. Cell Biol., 2010, 191, 463-470|
|Date||Deposition: Sep 15, 2010 / Header (metadata) release: Sep 24, 2010 / Map release: Oct 29, 2010 / Last update: Sep 19, 2012|
Downloads & links
|File||emd_1787.map.gz (map file in CCP4 format, 39367 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.8 Å|
CCP4 map header:
-Entire Microtubules co-polymerised with doublecortin and bound with kine...
|Entire||Name: Microtubules co-polymerised with doublecortin and bound with kinesin motor domain|
Number of components: 3 / Oligomeric State: 13-protofilament microtubule
-Component #1: protein, Alpha-beta tubulin dimer
|Protein||Name: Alpha-beta tubulin dimer / a.k.a: Tubulin dimer / Oligomeric Details: Heterodimer / Recombinant expression: No|
|Source||Species: Bos taurus / mammal / Bovine / ウシ /|
|Source (natural)||Location in cell: Cytoplasm / Organ or tissue: Brain|
-Component #2: protein, Doublecortin
|Protein||Name: Doublecortin / a.k.a: DCX / Oligomeric Details: Monomer / Recombinant expression: Yes|
|Source||Species: Homo sapiens / human|
|Source (engineered)||Expression System: Spodoptera frugiperda / arthropod / Vector: pFastBac|
|Source (natural)||Location in cell: Cytoplasm|
-Component #3: protein, Kinesin motor domain
|Protein||Name: Kinesin motor domain / a.k.a: Kinesin head / Oligomeric Details: Monomer / Recombinant expression: Yes|
|Source||Species: Rattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
|Source (natural)||Location in cell: Cytoplasm|
|Sample solution||Buffer solution: 80mM Pipes, 1mM EGTA, 3mM MgCl2, 1mM TCEP, 0.5mM GTP|
|Support film||300 mesh lacey carbon grids|
|Vitrification||Instrument: FEI VITROBOT / Cryogen name: ETHANE / Humidity: 100 % / Method: Chamber at 37 degrees C, blot 2s / Details: Vitrification instrument: Vitrobot (FEI)|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F20|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 15 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 50000 X (nominal)|
Astigmatism: Objective lens astigmatism was corrected at 150,000 times magnification
Cs: 2 mm / Imaging mode: BRIGHT FIELD / Defocus: 760 - 2900 nm
|Specimen Holder||Holder: Eucentric / Model: OTHER / Temperature: 93 K|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 63 / Scanner: ZEISS SCAI / Sampling size: 7 microns / Bit depth: 8 / Details: Images were binned with a factor of 2|
|Processing||Method: single particle reconstruction|
|3D reconstruction||Algorithm: Custom scripts, projection matching / Software: SPIDER, FREALIGN / CTF correction: FREALIGN|
Details: C1 map calculated from approximately 13,000 one-dimer-long microtubule segments
Resolution: 13.5 Å / Resolution method: FSC 0.5
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