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3F6N

Crystal structure of the virion-associated protein P3 from Caulimovirus

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID23-2
Synchrotron siteESRF
BeamlineID23-2
Temperature [K]100
Detector technologyCCD
Collection date2007-02-15
DetectorADSC QUANTUM 4
Wavelength(s)0.931
Spacegroup nameP 64
Unit cell lengths104.943, 104.943, 72.527
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.850 - 3.100
R-factor0.229
Rwork0.222
R-free0.28700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1t6f
RMSD bond length0.008
RMSD bond angle1.037
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwarePHASER
Refinement softwareREFMAC (5.5.0053)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0003.270
High resolution limit [Å]3.1003.100
Rmerge0.0650.306
Number of reflections8369
<I/σ(I)>16.54.6
Completeness [%]99.999.9
Redundancy5.45.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.529125% PEG 1000, 0.1M MES-NaOH buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K

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