|Entry||Database: EMDB / ID: 7099|
|Title||Cryo-EM structure of ATP-bound, outward-facing bovine multidrug resistance protein 1 (MRP1)|
|Sample||bovine multidrug resistance protein 1 (MRP1) E1454Q|
|Source||Bos taurus / mammal / Cattle /|
|Map data||Full map scaled to model, B-factor sharpened with a sharpening factor of -75 A^2.|
|Method||single particle reconstruction, at 3.14 Å resolution|
|Authors||Johnson ZL / Chen J|
|Citation||Cell, 2018, 172, 81-89.e10|
|Validation Report||PDB-ID: 6bhu|
SummaryFull reportAbout validation report
|Date||Deposition: Oct 31, 2017 / Header (metadata) release: Nov 22, 2017 / Map release: Dec 27, 2017 / Last update: Jan 24, 2018|
Downloads & links
|File||emd_7099.map.gz (map file in CCP4 format, 226493 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 0.817 Å|
CCP4 map header:
+Entire bovine multidrug resistance protein 1 (MRP1) E1454Q
|Entire||Name: bovine multidrug resistance protein 1 (MRP1) E1454Q / Number of components: 5|
|Mass||Theoretical: 170 kDa|
+Component #1: protein, bovine multidrug resistance protein 1 (MRP1) E1454Q
|Protein||Name: bovine multidrug resistance protein 1 (MRP1) E1454Q / Recombinant expression: No|
|Mass||Theoretical: 170 kDa|
|Source||Species: Bos taurus / mammal / Cattle /|
|Source (engineered)||Expression System: Homo sapiens / human / / Vector: Baculovirus / Cell of expression system: HEK293S GntI-|
+Component #2: protein, Multidrug resistance-associated protein 1
|Protein||Name: Multidrug resistance-associated protein 1 / Recombinant expression: No|
|Mass||Theoretical: 183.074062 kDa|
|Source (engineered)||Expression System: Bos taurus / mammal / Cattle /|
+Component #3: ligand, ADENOSINE-5'-TRIPHOSPHATE
|Ligand||Name: ADENOSINE-5'-TRIPHOSPHATE / Number of Copies: 2 / Recombinant expression: No|
|Mass||Theoretical: 0.507181 kDa|
+Component #4: ligand, MAGNESIUM ION
|Ligand||Name: MAGNESIUM ION / Number of Copies: 2 / Recombinant expression: No|
|Mass||Theoretical: 2.430505 MDa|
+Component #5: ligand, CHOLESTEROL
|Ligand||Name: CHOLESTEROL / Number of Copies: 3 / Recombinant expression: No|
|Mass||Theoretical: 0.386654 kDa|
|Sample solution||Specimen conc.: 4.9 mg/ml / pH: 8|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 295 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 84 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 37000 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 700 - 2400 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature: K ( 80 - 100 K)|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Image acquisition||Number of digital images: 4210|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 354752|
|3D reconstruction||Software: FREALIGN / Resolution: 3.14 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
-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
-Jul 12, 2017. Major update of PDB
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