|Entry||Database: PDB / ID: 5uow|
|Title||Triheteromeric NMDA receptor GluN1/GluN2A/GluN2B in complex with glycine, glutamate, MK-801 and a GluN2B-specific Fab, at pH 6.5|
|Descriptor||Ionotropic glutamate receptor subunit NR2B|
(N-methyl-D-aspartate receptor subunit ...) x 2
|Keywords||MEMBRANE PROTEIN / membrane protein|
|Specimen source||Xenopus laevis / amphibia / African clawed frog / |
Mus musculus / mammal / ハツカネズミ, はつかねずみ /
|Method||Electron microscopy (4.5 Å resolution / Particle / Single particle)|
|Authors||Lu, W. / Du, J. / Goehring, A. / Gouaux, E.|
|Citation||Science, 2017, 355|
SummaryFull reportAbout validation report
|Date||Deposition: Feb 1, 2017 / Release: Mar 22, 2017|
Downloads & links
A: N-methyl-D-aspartate receptor subunit NR1-8a
B: N-methyl-D-aspartate receptor subunit NR2A
C: N-methyl-D-aspartate receptor subunit NR1-8a
D: Ionotropic glutamate receptor subunit NR2B
F: GluN2B-specific Fab, termed 11D1
G: GluN2B-specific Fab, termed 11D1
-N-methyl-D-aspartate receptor subunit ... , 2 types, 3 molecules A
Mass: 91639.867 Da / Num. of mol.: 2 / Source: (gene. exp.) Xenopus laevis / References: UniProt: C0KD18
Mass: 93664.344 Da / Num. of mol.: 1 / Source: (gene. exp.) Xenopus laevis / References: UniProt: B7ZSK1
-Polypeptide(L) , 2 types, 3 molecules D
Mass: 94552.234 Da / Num. of mol.: 1 / Source: (gene. exp.) Xenopus laevis / References: UniProt: A7XY94
Mass: 18400.619 Da / Num. of mol.: 2 / Source: (gene. exp.) Mus musculus
-Non-polymers , 3 types, 18 molecules
|#6: Chemical||ChemComp-GLU / ||#7: Chemical||ChemComp-BMK / (|
|Sequence details||Sample sequence for this chains is unknown|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE|
|Component||Name: membrane protein / Type: COMPLEX / Entity ID: 1, 2, 3, 4, 5, 6 / Source: RECOMBINANT|
|Source (natural)||Organism: Xenopus laevis|
|Source (recombinant)||Organism: Homo sapiens|
|Buffer solution||pH: 6.5|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELD|
|Image recording||Electron dose: 0.84 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|3D reconstruction||Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 302052 / Symmetry type: POINT|
|Least-squares process||Highest resolution: 4.5 Å|
-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.
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- 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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