|Entry||Database: EMDB / ID: 3417|
|Title||Structure of tetrameric MotA complex|
|Keywords||Flagella motor / Stator / Single Particle analysis / Proton motive force|
|Sample||Aquifex aeolicus MotA|
|Source||Aquifex aeolicus / bacteria|
|Map data||Reconstruction of Aquifex aeolicus stator protein, tetrameric MotA complex|
|Method||single particle reconstruction, at 25 Å resolution|
|Authors||Takekawa N / Terahara N / Kato T / Gohara M / Mayanagi K / Hijikata A / Onoue Y / Kojima S / Shirai T / Namba K / Homma M|
|Citation||Sci Rep, 2016, 6, 31526-31526|
Sci Rep, 2016, 6, 31526-31526 Yorodumi Papers
|Date||Deposition: Apr 27, 2016 / Header (metadata) release: May 18, 2016 / Map release: Aug 2, 2017 / Last update: Aug 2, 2017|
Downloads & links
|File||emd_3417.map.gz (map file in CCP4 format, 1025 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.8 Å|
CCP4 map header:
-Entire Aquifex aeolicus MotA
|Entire||Name: Aquifex aeolicus MotA / Number of components: 1 / Oligomeric State: tetramer|
|Mass||Theoretical: 109 kDa|
-Component #1: protein, Motility protein A
|Protein||Name: Motility protein A / a.k.a: Chemotaxis protein MotA / Oligomeric Details: Tetramer / Recombinant expression: Yes / Number of Copies: 4|
|Mass||Theoretical: 109 kDa|
|Source||Species: Aquifex aeolicus / bacteria / Strain: VF5|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 / |
Vector: pColdI / Strain: BL21-CodonPlus(DE3)-RIPL
|External references||UniProt: UniProt: O67122|
|Sample solution||Specimen conc.: 0.1 mg/ml / Buffer solution: 50 mM Tris-HCl, 200 mM NaCl, 0.02% DMNG / pH: 8|
|Support film||200 mesh copper grid with continuous carbon suport, glow discharged|
|Staining||2% w/v uranyl acetate|
|Vitrification||Instrument: NONE / Cryogen name: NONE|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 3200FSC / Date: Nov 16, 2015|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 2.8 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 80000 X (nominal), 107140 X (calibrated) / Cs: 4.1 mm / Imaging mode: BRIGHT FIELD / Defocus: 1135 - 2200 nm / Energy filter: Omega Filter / Energy window: 0-20 eV|
|Specimen Holder||Holder: Nitrogen cooled / Model: JEOL 3200FSC CRYOHOLDER / Temperature: 85.5 K ( 85.5 - 85.7 K)|
|Camera||Detector: TVIPS TEMCAM-F415 (4k x 4k)|
|Image acquisition||Number of digital images: 50|
|Processing||Method: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 5419|
|3D reconstruction||Software: Relion-1.4 / Resolution: 25 Å / Resolution method: FSC 0.143|
-Oct 4, 2017. Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
- Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
- Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images).
- Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK) was determined the first biomolecule structure by EM. The first EM entry in PDB, PDB-1brd is determinedby him.
External links: The 2017 Nobel Prize in Chemistry - Press Release
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