|Entry||Database: EMDB / ID: 2676|
|Title||Electron cryo-microscopy of bovine ComplexI|
|Map data||Reconstruction of bovine ComplexI|
|Keywords||NADH dehydrogenase / respiratory complex|
|Source||Bos taurus (cattle)|
|Method||single particle reconstruction / cryo EM / 4.95 Å resolution|
|Authors||Vinothkumar KR / Zhu J / Hirst J|
|Citation||Journal: Nature / Year: 2014|
Title: Architecture of mammalian respiratory complex I.
Authors: Kutti R Vinothkumar / Jiapeng Zhu / Judy Hirst
|Validation Report||PDB-ID: 4uq8|
SummaryFull reportAbout validation report
|Date||Deposition: Jun 13, 2014 / Header (metadata) release: Jul 9, 2014 / Map release: Sep 17, 2014 / Last update: Jul 15, 2015|
|Structure viewer||EM map: |
Downloads & links
|File||emd_2676.map.gz (map file in CCP4 format, 85751 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.717 Å|
CCP4 map header:
-Entire NADH:ubiquinone oxidoreductase
|Entire||Name: NADH:ubiquinone oxidoreductase|
Details: The enzyme was isolated from bovine heart mitochondria in detergent micelles and imaged on ice as single particles
Number of components: 1 / Oligomeric State: 1
|Mass||Theoretical: 1000 kDa / Experimental: 1000 kDa|
-Component #1: protein, NADH:ubiquinone oxidoreductase
|Protein||Name: NADH:ubiquinone oxidoreductase / a.k.a: Complex IRespiratory complex I / Oligomeric Details: 1 / Recombinant expression: No / Number of Copies: 1|
|Mass||Theoretical: 1000 kDa / Experimental: 1000 kDa|
|Source||Species: Bos taurus (cattle)|
|Source (natural)||Organelle: mitochondria / Location in cell: mitochondrial inner membrane|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 3.5 mg/ml / Buffer solution: 20mM Tris-HCl, 150 mM NaCl, 0.03% Cymal-7 / pH: 8|
|Support film||300 mesh holey-carbon Quantifoil gold grid R 0.6/1 glow discharged in air|
|Vitrification||Instrument: OTHER / Cryogen name: ETHANE / Temperature: 100 K / Humidity: 100 %|
Method: The specimen was vitrified in an environmental plunge-freeze apparatus (Bellare et al, J.Electr. Micros. Tech., 1988, 10, 87-111). Blot for 15-18 seconds after the diameter of the blotted meniscus ceases to expand and plunged.
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: Oct 21, 2013|
Details: Exposure intensity set to give 50 electron/pixel/second at the detector, which translates to ~17 electrons/square_Angstrom/second at the specimen. Each image was exposed for 4 seconds.
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 64 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 47000 X (nominal), 81495 X (calibrated)|
Astigmatism: Objective lens astigmatism was corrected at 120,000 times magnification once at the start of data collection
Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 2000 - 5000 nm
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature: 85 K ( 80 - 90 K)|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 1154 / Sampling size: 14 microns|
Details: An in-house built system was used to intercept the frames from the detector at a rate of 18 frames per second.
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