|Entry||Database: PDB / ID: 5v4s|
|Title||CryoEM Structure of a Prokaryotic Cyclic Nucleotide-Gated Ion Channel|
cation channel family / cyclic nucleotide-binding domain multi-domain protein
|Keywords||TRANSPORT PROTEIN / Ion channel / cyclic nucleotide / allostery / vision / olfaction|
|Specimen source||Leptospira licerasiae serovar varillal str. var 010 / bacteria|
|Method||Electron microscopy (4.2 Å resolution / Particle / Single particle)|
|Authors||James, Z.M. / Borst, A.J. / Haitin, Y. / Frenz, B. / DiMaio, F. / Zagotta, W.N. / Veesler, D.|
|Citation||Proc. Natl. Acad. Sci. U.S.A., 2017, 114, 4430-4435|
Proc. Natl. Acad. Sci. U.S.A., 2017, 114, 4430-4435 Yorodumi Papers
SummaryFull reportAbout validation report
|Date||Deposition: Mar 10, 2017 / Release: Apr 12, 2017|
Downloads & links
A: Transporter, cation channel family / cyclic nucleotide-binding domain multi-domain protein
B: Transporter, cation channel family / cyclic nucleotide-binding domain multi-domain protein
C: Transporter, cation channel family / cyclic nucleotide-binding domain multi-domain protein
D: Transporter, cation channel family / cyclic nucleotide-binding domain multi-domain protein
Mass: 53464.785 Da / Num. of mol.: 4
Source: (gene. exp.) Leptospira licerasiae serovar varillal str. var 010 / bacteria
References: UniProt: I0XVQ9
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE|
|Component||Name: LliK / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Value: 0.2 deg. / Units: MEGADALTONS / Experimental value: NO|
|Source (natural)||Organism: Leptospira licerasiae serovar Varillal str. VAR 010|
|Source (recombinant)||Organism: Escherichia coli|
|Buffer solution||pH: 7.9|
|Specimen||Conc.: 0.9 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid mesh size: 400 / Grid type: Quantifoil R1.2/1.3|
|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: 1.4 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Particle selection||Number of particles selected: 379000|
|Symmetry||Point symmetry: C4|
|3D reconstruction||Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 18737 / Symmetry type: POINT|
|Atomic model building||Ref protocol: OTHER / Ref space: REAL|
-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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