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- EMDB-5181: The structure of avian polyomavirus (empty capsids) treated with ... -

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Basic information

Database: EMDB / ID: 5181
TitleThe structure of avian polyomavirus (empty capsids) treated with 250 mM L-arginine
Map dataCryo-EM based reconstruction of avian polyomavirus empty capsids
Sampleavian polyomavirus with 250 mM L-arginine:
Keywordsavian / polyomavirus / VP4
Sourceavian polyomavirus (avian polyomavirus)
Methodsingle particle reconstruction / cryo EM / 17.3 Å resolution
AuthorsShen PS / Enderlein D / Nelson C / Carter WS / Kawano M / Xing L / Swenson RD / Olson NH / Baker TS / Cheng RH / Atwood WJ / Johne R / Belnap DM
CitationJournal: Virology / Year: 2011
Title: The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4.
Authors: Peter S Shen / Dirk Enderlein / Christian D S Nelson / Weston S Carter / Masaaki Kawano / Li Xing / Robert D Swenson / Norman H Olson / Timothy S Baker / R Holland Cheng / Walter J Atwood / Reimar Johne / David M Belnap
Abstract: Avian polyomavirus (APV) causes a fatal, multi-organ disease among several bird species. Using cryogenic electron microscopy and other biochemical techniques, we investigated the structure of APV and ...Avian polyomavirus (APV) causes a fatal, multi-organ disease among several bird species. Using cryogenic electron microscopy and other biochemical techniques, we investigated the structure of APV and compared it to that of mammalian polyomaviruses, particularly JC polyomavirus and simian virus 40. The structure of the pentameric major capsid protein (VP1) is mostly conserved; however, APV VP1 has a unique, truncated C-terminus that eliminates an intercapsomere-connecting β-hairpin observed in other polyomaviruses. We postulate that the terminal β-hairpin locks other polyomavirus capsids in a stable conformation and that absence of the hairpin leads to the observed capsid size variation in APV. Plug-like density features were observed at the base of the VP1 pentamers, consistent with the known location of minor capsid proteins VP2 and VP3. However, the plug density is more prominent in APV and may include VP4, a minor capsid protein unique to bird polyomaviruses.
DateDeposition: Apr 9, 2010 / Header (metadata) release: Dec 8, 2010 / Map release: Jan 19, 2011 / Last update: Dec 3, 2014

Structure visualization

  • Surface view with section colored by density value
  • Surface level: 20.3
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 20.3
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
Supplemental images

Downloads & links


Fileemd_5181.map.gz (map file in CCP4 format, 193091 KB)
Projections & slices

Image control

AxesZ (Sec.)Y (Row.)X (Col.)
367 pix
1.57 Å/pix.
= 598.17 Å
367 pix
1.57 Å/pix.
= 598.17 Å
367 pix
1.57 Å/pix.
= 598.17 Å



Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.57 Å
Contour Level:20.3 (by author), 20.3 (movie #1):
Minimum - Maximum-26.44575691 - 71.30140686
Average (Standard dev.)5.23682499 (15.14913940)


Space Group Number1
Map Geometry
Axis orderXYZ
CellA=B=C: 598.17004 Å
α=β=γ: 90.0 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.571.571.57
M x/y/z381381381
origin x/y/z0.0000.0000.000
length x/y/z598.170598.170598.170
start NX/NY/NZ-34-26-72
MAP C/R/S123
start NC/NR/NS-183-183-183
D min/max/mean-26.44671.3015.237

Supplemental data

Sample components

Entire avian polyomavirus with 250 mM L-arginine

EntireName: avian polyomavirus with 250 mM L-arginine / Number of components: 1 / Oligomeric State: virions

Component #1: virus, avian polyomavirus

VirusName: avian polyomavirus / a.k.a: avian polyomavirus / Class: VIRION
Details: Cryo-EM of avian polyomavirus over holey carbon grids
Empty: Yes / Enveloped: No / Isolate: STRAIN
SpeciesSpecies: avian polyomavirus (avian polyomavirus)
Source (natural)Host category: VERTEBRATES
Shell #1Name of element: VP1 / Diameter: 5000 Å / T number(triangulation number): 7

Experimental details

Sample preparation

SpecimenSpecimen state: particle / Method: cryo EM
Sample solutionBuffer solution: 200 mM NaCl, 20 mM Tris-HCl, 1 mM CaCl2 buffer, 250 mM L-arginine, pH 10.7
pH: 10.7
Support film200 mesh copper grid (holey carbon)
Stainingno stain (cryo-EM)
VitrificationInstrument: FEI VITROBOT / Cryogen name: ETHANE / Temperature: 89 K / Humidity: 100 % / Method: 1 second blot before plunging
Details: Vitrification instrument: Vitrobot. vitrification carried out in nitrogen atmosphere

Electron microscopy imaging

Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company
ImagingMicroscope: FEI TECNAI F30 / Date: Apr 23, 2007
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
LensMagnification: 39000 X (nominal), 39000 X (calibrated)
Astigmatism: astigmatism was corrected at 59,000 times magnification
Cs: 2 mm / Imaging mode: BRIGHT FIELD / Defocus: 500 - 4900 nm
Specimen HolderHolder: Side entry liquid nitrogen-cooled cryo specimen holder
Model: GATAN LIQUID NITROGEN / Temperature: 90 K ( 88 - 95 K)
CameraDetector: KODAK SO-163 FILM

Image acquisition

Image acquisitionNumber of digital images: 88 / Scanner: NIKON SUPER COOLSCAN 9000 / Sampling size: 1.57 microns / Bit depth: 16 / Details: Micrographs digitized in positive contrast mode.

Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: I (icosahedral)
3D reconstructionAlgorithm: common lines / Software: PFT2, EM3DR2 / CTF correction: each micrograph / Resolution: 17.3 Å / Resolution method: FSC 0.333

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