3SU3
Crystal structure of NS3/4A protease 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 | 55.095, 58.461, 60.250 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.380 - 1.300 |
R-factor | 0.1653 |
Rwork | 0.164 |
R-free | 0.18230 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.445 |
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 | 1.350 |
High resolution limit [Å] | 1.300 | 2.800 | 1.300 |
Rmerge | 0.052 | 0.031 | 0.329 |
Number of reflections | 46251 | ||
<I/σ(I)> | 12 | ||
Completeness [%] | 95.7 | 97.1 | 85.7 |
Redundancy | 4.2 | 4.2 | 3.7 |
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 |