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4MWF

Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL12-2
Synchrotron siteSSRL
BeamlineBL12-2
Temperature [K]100
Detector technologyCCD
Collection date2013-01-19
DetectorMARMOSAIC 325 mm CCD
Wavelength(s)1.033
Spacegroup nameP 21 21 21
Unit cell lengths47.132, 166.553, 209.963
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution49.078 - 2.645
R-factor0.2333
Rwork0.231
R-free0.27020
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.275
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwarePHENIX ((phenix.refine: 1.8.2_1309))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]49.0902.700
High resolution limit [Å]2.6502.650
Number of reflections46174
Completeness [%]93.476.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.529320% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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