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4DGV

Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody HCV1, P2(1) form

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-D
Synchrotron siteAPS
Beamline23-ID-D
Temperature [K]100
Detector technologyCCD
Collection date2011-08-17
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)1.033
Spacegroup nameP 1 21 1
Unit cell lengths44.041, 75.301, 60.800
Unit cell angles90.00, 91.53, 90.00
Refinement procedure
Resolution44.025 - 1.805
R-factor0.1723
Rwork0.170
R-free0.21390
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3giz
RMSD bond length0.007
RMSD bond angle1.208
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwarePHENIX ((phenix.refine: 1.7.2_869))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]75.3011.840
High resolution limit [Å]1.8051.805
Number of reflections36325
<I/σ(I)>9.83
Completeness [%]99.899.5
Redundancy3.63.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP29340 mM potassium dihydrogen phosphate, 20% glycerol, 16% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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