4U01
HCV NS3/4A serine protease in complex with 6570
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2007-12-14 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.007 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 150.034, 174.363, 133.010 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.230 - 2.800 |
| R-factor | 0.23618 |
| Rwork | 0.233 |
| R-free | 0.28986 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.189 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.230 | 3.000 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.086 | 0.619 |
| Number of reflections | 41817 | |
| <I/σ(I)> | 11.77 | |
| Completeness [%] | 96.8 | 96.4 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | PEG |
