8QP6
Crystal structure of Hepatitis C Virus E1 glycoprotein epitope 314-324 scaffold design 1W4K_08 in complex with neutralizing antibody F(ab) fragment IGH526
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 | 2019-03-15 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.0007 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.320, 121.760, 234.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.630 - 2.590 |
R-factor | 0.234 |
Rwork | 0.232 |
R-free | 0.27310 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.583 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHENIX (1.18_3861) |
Refinement software | PHENIX (1.18_3861) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.630 | 2.686 |
High resolution limit [Å] | 2.590 | 2.593 |
Number of reflections | 64890 | 6325 |
<I/σ(I)> | 11.18 | 0.74 |
Completeness [%] | 99.4 | 97.58 |
Redundancy | 13.6 | 13.7 |
CC(1/2) | 0.997 | 0.564 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.2 M Ammonium acetate 0.1 M BIS-Tris 5.5 25 % w/v PEG 3350 |