|Entry||Database: EMDB / ID: 8823|
|Title||Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin|
|Sample||Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin|
|Source||Rattus norvegicus / mammal / Brown rat (Wikipedia) /|
|Map data||Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin|
|Method||single particle reconstruction, at 4.2 Å resolution|
|Authors||Twomey EC / Yelshanskaya MV|
|Citation||Nature, 2017, 549, 60-65|
|Validation Report||PDB-ID: 5weo|
SummaryFull reportAbout validation report
|Date||Deposition: Jul 10, 2017 / Header (metadata) release: Aug 2, 2017 / Map release: Aug 2, 2017 / Last update: Sep 13, 2017|
Downloads & links
|File||emd_8823.map.gz (map file in CCP4 format, 108001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.08 Å|
CCP4 map header:
-Entire Activated GluA2 complex bound to glutamate, cyclothiazide, and ST...
|Entire||Name: Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin|
Number of components: 4
-Component #1: protein, Activated GluA2 complex bound to glutamate, cyclothiazid...
|Protein||Name: Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin|
Recombinant expression: No
|Source||Species: Rattus norvegicus / mammal / Brown rat (Wikipedia) /|
|Source (engineered)||Expression System: Homo sapiens / human / Wikipedia / Cell of expression system: HEK293 gnti-|
-Component #2: protein, Glutamate receptor 2,Voltage-dependent calcium channel g...
|Protein||Name: Glutamate receptor 2,Voltage-dependent calcium channel gamma-2 subunit chimera|
Recombinant expression: No
|Mass||Theoretical: 115.501969 kDa|
|Source (engineered)||Expression System: Mus musculus / mammal / House mouse (Wikipedia) /|
-Component #3: ligand, GLUTAMIC ACID
|Ligand||Name: GLUTAMIC ACID / Number of Copies: 4 / Recombinant expression: No|
|Mass||Theoretical: 0.147129 kDa|
-Component #4: ligand, CYCLOTHIAZIDE
|Ligand||Name: CYCLOTHIAZIDE / Number of Copies: 4 / Recombinant expression: No|
|Mass||Theoretical: 0.389878 kDa|
|Sample solution||Specimen conc.: 4 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: 55 e/Å2 / Illumination mode: SPOT SCAN|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 69207|
|3D reconstruction||Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF|
Details: TMD map uploaded under additional files is at 4.0 angstrom resolution.
-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
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