|Entry||Database: PDB / ID: 6eny|
|Title||Structure of the human PLC editing module|
Protein disulfide-isomerase A3
HLA class I histocompatibility antigen
A-3 alpha chain
|Keywords||IMMUNE SYSTEM / adaptive immunity / antigen processing / chaperone / MHC class I|
|Specimen source||Homo sapiens / human|
|Method||Electron microscopy (5.8 Å resolution / Particle / Single particle)|
|Authors||Trowitzsch, S. / Januliene, D. / Blees, A. / Moeller, A. / Tampe, R.|
|Citation||Nature, 2017, 551, 525-528|
SummaryFull reportAbout validation report
|Date||Deposition: Oct 7, 2017 / Release: Nov 29, 2017|
Downloads & links
D: Protein disulfide-isomerase A3
F: HLA class I histocompatibility antigen, A-3 alpha chain
-Polypeptide(L) , 5 types, 5 molecules B
C D F G
Mass: 11748.160 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens / References: UniProt: P61769
Mass: 45761.184 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens / References: UniProt: O15533
Mass: 54341.102 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens / References: UniProt: P30101, EC: 220.127.116.11
Mass: 38363.535 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens / References: UniProt: P04439
Mass: 46507.145 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens / References: UniProt: P27797
-Non-polymers , 3 types, 6 molecules
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE|
|Component||Name: Protein Complex / Type: COMPLEX / Entity ID: 1, 2, 3, 4, 5 / Source: NATURAL|
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Homo sapiens|
|Buffer solution||pH: 7.5|
|Specimen||Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid type: C-flat-2/2|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 kelvins|
-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: 55 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 QUANTUM (4k x 4k)|
|CTF correction||Details: CTF correction was performed internally in Relion and Frealign|
|Symmetry||Point symmetry: C1|
|3D reconstruction||Resolution: 5.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 141078 / Symmetry type: POINT|
|Least-squares process||Highest resolution: 5.8 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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