2B60
Structure of HIV-1 protease mutant bound to Ritonavir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 61 |
| Unit cell lengths | 61.979, 61.979, 84.247 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| Rwork | 0.216 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.103 | 0.443 |
| Number of reflections | 9267 | |
| <I/σ(I)> | 2.3 | |
| Completeness [%] | 98.8 | 98.8 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.5 | 298 | 20 mM Sodium Acetate and 1 M Ammonium Sulfate, pH 5.5, VAPOR DIFFUSION, temperature 298K |
