8QP7
Crystal structure of Hepatitis C Virus E2 glycoprotein epitopeI 411-424 scaffold design 4CIL_04
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 2 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-12-15 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.999995 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 60.290, 31.670, 135.750 |
Unit cell angles | 90.00, 94.31, 90.00 |
Refinement procedure
Resolution | 30.060 - 2.050 |
R-factor | 0.2168 |
Rwork | 0.214 |
R-free | 0.26170 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.468 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.18_3861) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.060 | 2.123 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 16198 | 1652 |
<I/σ(I)> | 9.85 | 2.54 |
Completeness [%] | 97.2 | 95.02 |
Redundancy | 4.5 | |
CC(1/2) | 0.980 | 0.323 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 25% (w/v) PEG 1500, 100 mM MMT buffer pH 9.0 |