4DGY
Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody HCV1, C2 form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 141.099, 63.065, 69.300 |
| Unit cell angles | 90.00, 95.72, 90.00 |
Refinement procedure
| Resolution | 28.764 - 1.798 |
| R-factor | 0.1893 |
| Rwork | 0.188 |
| R-free | 0.22130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3giz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.074 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.2_869)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.198 | 1.860 |
| High resolution limit [Å] | 1.798 | 1.798 |
| Number of reflections | 55279 | |
| <I/σ(I)> | 13.4 | 3 |
| Completeness [%] | 98.9 | 100 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 25% PEG4000, 0.2 M ammonium sulfate, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
