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- EMDB-52400: Localized reconstruction of asymmetric unit from transcribing sin... -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-52400
TitleLocalized reconstruction of asymmetric unit from transcribing single-layered particle of bacteriophage phi6
Map data
Sample
  • Virus: Cystovirus phi6
    • Protein or peptide: Major inner protein P1
    • Protein or peptide: NTPase
Keywordscystovirus / phi6 / semi-conservative transcription / cryo-EM / cryogenic electron microscopy / localized reconstruction / symmetry relaxation / virus / dsRNA virus / bacteriophage
Function / homology
Function and homology information


T=2 icosahedral viral capsid / viral genome packaging / viral inner capsid / viral nucleocapsid / RNA binding / identical protein binding
Similarity search - Function
: / Major inner capsid protein P1 / Packaging enzyme P4 / ATPase P4 of dsRNA bacteriophage phi-12 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Major inner protein P1 / NTPase
Similarity search - Component
Biological speciesCystovirus phi6
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsIlca SL / Huiskonen JT
Funding support Finland, 1 items
OrganizationGrant numberCountry
Academy of Finland331627 Finland
CitationJournal: To be published
Title: Restructuring of bacteriophage phi6 viral particle activates semi-conservative transcription
Authors: Ilca SL / Sun X / Kumpula E-P / Eskelin K / Poranen MM / Huiskonen JT
History
DepositionDec 20, 2024-
Header (metadata) releaseJan 14, 2026-
Map releaseJan 14, 2026-
UpdateJan 14, 2026-
Current statusJan 14, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_52400.map.gz / Format: CCP4 / Size: 11.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.4 Å/pix.
x 144 pix.
= 201.6 Å
1.4 Å/pix.
x 144 pix.
= 201.6 Å
1.4 Å/pix.
x 144 pix.
= 201.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.4 Å
Density
Contour LevelBy AUTHOR: 0.04
Minimum - Maximum-0.1809705 - 0.33341074
Average (Standard dev.)0.002176929 (±0.020257624)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions144144144
Spacing144144144
CellA=B=C: 201.59999 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_52400_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_52400_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_52400_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Cystovirus phi6

EntireName: Cystovirus phi6
Components
  • Virus: Cystovirus phi6
    • Protein or peptide: Major inner protein P1
    • Protein or peptide: NTPase

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Supramolecule #1: Cystovirus phi6

SupramoleculeName: Cystovirus phi6 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10879 / Sci species name: Cystovirus phi6 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: Yes / Virus empty: No
Virus shellShell ID: 1 / Name: Outer protein shell / T number (triangulation number): 13
Virus shellShell ID: 2 / Name: Inner protein shell / T number (triangulation number): 1

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Macromolecule #1: Major inner protein P1

MacromoleculeName: Major inner protein P1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Cystovirus phi6
Molecular weightTheoretical: 84.783359 KDa
SequenceString: MFNLKVKDLN GSARGLTQAF AIGELKNQLS VGALQLPLQF TRTFSASMTS ELLWEVGKGN IDPVMYARLF FQYAQAGGAL SVDELVNQF TEYHQSTACN PEIWRKLTAY ITGSSNRAIK ADAVGKVPPT AILEQLRTLA PSEHELFHHI TTDFVCHVLS P LGFILPDA ...String:
MFNLKVKDLN GSARGLTQAF AIGELKNQLS VGALQLPLQF TRTFSASMTS ELLWEVGKGN IDPVMYARLF FQYAQAGGAL SVDELVNQF TEYHQSTACN PEIWRKLTAY ITGSSNRAIK ADAVGKVPPT AILEQLRTLA PSEHELFHHI TTDFVCHVLS P LGFILPDA AYVYRVGRTA TYPNFYALVD CVRASDLRRM LTALSSVDSK MLQATFKAKG ALAPALISQH LANAATTAFE RS RGNFDAN AVVSSVLTIL GRLWSPSTPK ELDPSARLRN TNGIDQLRSN LALFIAYQDM VKQRGRAEVI FSDEELSSTI IPW FIEAMS EVSPFKLRPI NETTSYIGQT SAIDHMGQPS HVVVYEDWQF AKEITAFTPV KLANNSNQRF LDVEPGISDR MSAT LAPIG NTFAVSAFVK NRTAVYEAVS QRGTVNSNGA EMTLGFPSVV ERDYALDRDP MVAIAALRTG IVDESLEARA SNDLK RSMF NYYAAVMHYA VAHNPEVVVS EHQGVAAEQG SLYLVWNVRT ELRIPVGYNA IEGGSIRTPE PLEAIAYNKP IQPSEV LQA KVLDLANHTT SIHIWPWHEA STEFAYEDAY SVTIRNKRYT AEVKEFELLG LGQRRERVRI LKPTVAHAII QMWYSWF VE DDRTLAAARR TSRDDAEKLA IDGRRMQNAV TLLRKIEMIG TTGIGASAVH LAQSRIVDQM AGRGLIDDSS DLHVGINR H RIRIWAGLAV LQMMGLLSRS EAEALTKVLG DSNALGMVVA TTDID

UniProtKB: Major inner protein P1

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Macromolecule #2: NTPase

MacromoleculeName: NTPase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Cystovirus phi6
Molecular weightTheoretical: 4.134507 KDa
SequenceString:
PTSMKALDHT SIASVAPLER GSVDTDDRNS APRRGANFS

UniProtKB: NTPase

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 41.0 µm / Nominal defocus min: 2.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 391662
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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