3SU6
Crystal structure of NS3/4A protease variant A156T in complex with vaniprevir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Collection date | 2010-12-07 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.981, 58.451, 59.829 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.280 - 1.100 |
R-factor | 0.1508 |
Rwork | 0.150 |
R-free | 0.16530 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.363 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.140 |
High resolution limit [Å] | 1.100 | 2.370 | 1.100 |
Rmerge | 0.058 | 0.034 | 0.323 |
Number of reflections | 76300 | ||
<I/σ(I)> | 12.1 | ||
Completeness [%] | 96.6 | 96.5 | 77.7 |
Redundancy | 5.2 | 5.8 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | hanging drop, vapor diffusion | 6.2 | 295 | 20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, hanging drop, vapor diffusion, temperature 295K |