6WO5
Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 1a bound to neutralizing antibody 212.1.1 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 | 2018-05-05 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.97946 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.793, 242.204, 100.729 |
Unit cell angles | 90.00, 98.31, 90.00 |
Refinement procedure
Resolution | 47.435 - 2.619 |
R-factor | 0.2051 |
Rwork | 0.203 |
R-free | 0.24990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mwf |
RMSD bond length | 0.004 |
RMSD bond angle | 0.799 |
Data reduction software | HKL-2000 (3.25) |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.670 |
High resolution limit [Å] | 2.619 | 2.619 |
Number of reflections | 76536 | 2986 |
<I/σ(I)> | 16.3 | |
Completeness [%] | 96.2 | |
Redundancy | 4.8 | |
CC(1/2) | 0.960 | 0.880 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | from 20% (w/v) PEG 3000, 0.2M NaCl, 0.1M HEPES pH 7.5 |