6WOQ
Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 1a bound to neutralizing antibody HC1AM and non neutralizing antibody E1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-12 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.97946 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 200.744, 103.721, 196.149 |
Unit cell angles | 90.00, 113.65, 90.00 |
Refinement procedure
Resolution | 34.662 - 3.667 |
R-factor | 0.2291 |
Rwork | 0.227 |
R-free | 0.27730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mwf |
RMSD bond length | 0.006 |
RMSD bond angle | 0.915 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 3.760 |
High resolution limit [Å] | 3.667 | 3.667 |
Number of reflections | 33504 | 1171 |
<I/σ(I)> | 7.7 | |
Completeness [%] | 84.3 | |
Redundancy | 2.8 | |
CC(1/2) | 0.830 | 0.460 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 10% (w/v) PEG 8000, 0.2M MgCl2, 0.1M Tris, pH 7.0 |