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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | MS2 bacteriophage coat protein with waters modeled | ||||||||||||
![]() | Sharpened map, output from CryoSPARC non-uniform refinement. | ||||||||||||
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![]() | Bacteriophage / VLP / MS2 / VIRUS | ||||||||||||
Function / homology | ![]() negative regulation of viral translation / T=3 icosahedral viral capsid / regulation of translation / structural molecule activity / RNA binding / identical protein binding Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 1.75 Å | ||||||||||||
![]() | Zimanyi CM / Bobe D / Jenkins MC / Kopylov M | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Overcoming air-water interface-induced artifacts in Cryo-EM with protein nanocrates Authors: Jenkins MC / Bobe D / Johnston JD / Cheung J / Karasawa A / Zimanyi CM / Dermanci O / Finn MG / de Marco A / Kopylov M | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 23.2 KB 23.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.6 KB | Display | ![]() |
Images | ![]() | 160 KB | ||
Masks | ![]() | 421.9 MB | ![]() | |
Filedesc metadata | ![]() | 6.6 KB | ||
Others | ![]() ![]() ![]() | 206.1 MB 389.4 MB 389.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 24.6 KB | Display | |
Data in CIF | ![]() | 31.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9q1dMC ![]() 9q1bC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Sharpened map, output from CryoSPARC non-uniform refinement. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.829 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: Unsharpened map, output from CryoSPARC non-uniform refinement.
File | emd_72124_additional_1.map | ||||||||||||
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Annotation | Unsharpened map, output from CryoSPARC non-uniform refinement. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Unsharpened half map, output from CryoSPARC non-uniform refinement.
File | emd_72124_half_map_1.map | ||||||||||||
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Annotation | Unsharpened half map, output from CryoSPARC non-uniform refinement. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Unsharpened half map, output from CryoSPARC non-uniform refinement.
File | emd_72124_half_map_2.map | ||||||||||||
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Annotation | Unsharpened half map, output from CryoSPARC non-uniform refinement. | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Escherichia phage MS2 capsid protein
Entire | Name: Escherichia phage MS2 capsid protein |
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Components |
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-Supramolecule #1: Escherichia phage MS2 capsid protein
Supramolecule | Name: Escherichia phage MS2 capsid protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: Purified after recombinant expression in E. coli. |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Capsid protein
Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.738464 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ASNFTQFVLV DNGGTGDVTV APSNFANGVA EWISSNSRSQ AYKVTCSVRQ SSAQNRKYTI KVEVPKVATQ TVGGVELPVA AWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP SAIAANSGIY UniProtKB: Capsid protein |
-Macromolecule #2: water
Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 265 / 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: 8.5 / Details: 100 mM Tris-HCl [pH 8.5], 80 mM KCl, 10 mM MgCl2 |
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Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 7 sec. / Pretreatment - Atmosphere: OTHER |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 4960 / Average exposure time: 1.2 sec. / Average electron dose: 52.36 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.7000000000000001 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |