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Title:Three-dimensional structure of the bacteriophage P22 tail machine.
Authors:Tang L, Marion WR, Cingolani G, Prevelige PE, Johnson JE
Sample:the tail machine isolated from bacteriophage P22
Aggregation state:Single particle (23 angstroms resolution)
Red flagLatest update:2011-05-26
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Sample
Sample name: the tail machine isolated from bacteriophage P22
Oligomeric state: 12-, 6-, and 3-fold symmetry
Theoretical molecular weight of the sample: 2.8
Components:
ID Type Name Exp. MW (MDa) Oligomeric details Mutant Organism GO identifier InterPro identifier Virus identifier Details
1proteinportal82.611dodecamertrueDNA packaging
2proteintailspike71.857trimerfalsereceptor binding
3proteingp418.025dodecamerfalseforms a channel; transglycosylase
4proteingp1052.457hexamerfalseforms a channel
5proteingp2624.603trimerfalseneedle-like plug
Experiment
Sample preparation:
pHSample conc.DetailsStainingSample support details
8.0 mg/mL50 mM Na2HPO4, pH8.0300 mesh holey copper grid
Vitrification:
Cryogen nameHumidityTemp.Instr.MethodTime resolvedDetails
ETHANE%89 Khome-made plungerblot for 3-4 seconds before plunging ms
Imaging:
MicroscopeVoltageIllumination modeImaging modeCsDefocus min.Defocus max.Nominal mag.Calibrated mag.Electron sourceDetectorDetector distanceAstigmatism
FEI/PHILIPS CM200FEG120 kVOTHERBRIGHT FIELD2.0 mm nm nm50000FIELD EMISSION GUNKodak SO163 film mmobjective lens astigmatism was corrected at 105,000 times magnification

Specimen holderHolder modelTilt min.Tilt max.Energy filterEnergy windowTemp.Temp. min.Temp. max.Beam tiltElectron doseOther detailsDate
Side entry liquid nitrogen-cooled cryo specimen holderGATAN LIQUID NITROGEN60° eV89 K K K mrad e/Å22004-05-19
Processing
Software:spider
Resolution by author:23 Å
Resolution method:FSC at 0.5 cut-off
Unit cell:
Scanned images:
Num. imagesSampling sizeOD rangeQuant. bit numberOther detailsScanner
547 μm/pixel8linkZEISS SCAI
Fitting:
PDBProtocolTarget crit.SoftwareB valueFitting spacePDB chainDetails
1TYX 1LKT rigid bodycorrelation coefficientcoloresREALThe receptor-binding domain (1TYX) of the tailspike was computationally docked with the program colores, and the docking was unambiguous. Then the head-binding domain (1LKT) was manually docked.
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