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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | HcCCR in NaCl | |||||||||
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![]() | channelrhodopsin / MEMBRANE PROTEIN | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.37 Å | |||||||||
![]() | Zhang MF | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Structure of HcCCR Authors: Zhang MF | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.2 KB 13.2 KB | Display Display | ![]() |
Images | ![]() | 135 KB | ||
Filedesc metadata | ![]() | 5.1 KB | ||
Others | ![]() ![]() | 391.3 MB 391.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 18.1 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.57 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_35423_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35423_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : HcCCR
Entire | Name: HcCCR |
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Components |
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-Supramolecule #1: HcCCR
Supramolecule | Name: HcCCR / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: HcCCR
Macromolecule | Name: HcCCR / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 30.224213 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MPFCGGRPED GWHHGSIHDM DYPLLGAMAA ICSVFIGGSG AWMLYRLDLG LGYSCKPHHS GYAPEANSFS ALSCLVSGTI YAAKTFDFF DGGGTPFSFN WYWYLDYVFT CPLILLDVLY TLEIPHKLRF VFAVIITLWC GVAAFVTPSA FRFGYYAVGC V WFVPFSFS ...String: MPFCGGRPED GWHHGSIHDM DYPLLGAMAA ICSVFIGGSG AWMLYRLDLG LGYSCKPHHS GYAPEANSFS ALSCLVSGTI YAAKTFDFF DGGGTPFSFN WYWYLDYVFT CPLILLDVLY TLEIPHKLRF VFAVIITLWC GVAAFVTPSA FRFGYYAVGC V WFVPFSFS LLRHVKQRYQ VYPPKCQKIL FWACTIFFGF WPLFPILFLF SWLGTGHIDQ QAFTIIHAFL DLFCKTVFGL IM TFFRLEL EEHTEVLGLP LNEPKGKH |
-Macromolecule #2: RETINAL
Macromolecule | Name: RETINAL / type: ligand / ID: 2 / Number of copies: 3 / Formula: RET |
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Molecular weight | Theoretical: 284.436 Da |
Chemical component information | ![]() ChemComp-RET: |
-Macromolecule #3: SODIUM ION
Macromolecule | Name: SODIUM ION / type: ligand / ID: 3 / Number of copies: 48 |
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Molecular weight | Theoretical: 22.99 Da |
-Macromolecule #4: (1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadeca...
Macromolecule | Name: (1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate type: ligand / ID: 4 / Number of copies: 6 / Formula: L9Q |
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Molecular weight | Theoretical: 746.05 Da |
Chemical component information | ![]() ChemComp-L9Q: |
-Macromolecule #5: water
Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 33 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.37 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 267000 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |