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2V33

High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]120
Detector technologyCCD
Collection date2005-11-04
DetectorADSC CCD
Spacegroup nameC 2 2 21
Unit cell lengths60.343, 62.659, 113.735
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.570 - 1.550
R-factor0.199
Rwork0.198
R-free0.22600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1RER (DOMAIN III)
RMSD bond length0.010
RMSD bond angle1.369
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.5701.550
High resolution limit [Å]1.5501.500
Rmerge0.0500.560
Number of reflections31583
<I/σ(I)>23.7
Completeness [%]98.895.9
Redundancy4.43.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.525% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP

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