4WHY
Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody 3/11, P21 crystal form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-03-20 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97902 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.760, 205.510, 69.020 |
Unit cell angles | 90.00, 103.18, 90.00 |
Refinement procedure
Resolution | 47.970 - 2.620 |
R-factor | 0.2067 |
Rwork | 0.204 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.250 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | BUSTER (2.11.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.760 |
High resolution limit [Å] | 2.620 | 2.620 |
Rmerge | 0.444 | |
Number of reflections | 51028 | |
<I/σ(I)> | 9.9 | 1.6 |
Completeness [%] | 97.0 | 87.5 |
Redundancy | 3.2 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 100 mM TRIS, 66% MPD |