4XVJ
STRUCTURE OF THE HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 ANTIGENIC 2 REGION 412-423 BOUND TO THE BROADLY NEUTRALIZING ANTIBODY HC33.1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | SIEMENS |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2014-11-09 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.541 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.085, 53.728, 107.238 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.27400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.060 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.084 | 0.396 |
| Number of reflections | 14203 | |
| <I/σ(I)> | 13.3 | 4.3 |
| Completeness [%] | 94.9 | 88.9 |
| Redundancy | 9.33 | 8.66 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | PEG 8000, MPD |
