3NU3
Wild Type HIV-1 Protease with Antiviral Drug Amprenavir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.107, 85.971, 46.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.020 |
| R-factor | 0.1228 |
| Rwork | 0.123 |
| R-free | 0.14160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qci |
| RMSD bond length | 0.017 |
| RMSD bond angle | 0.036 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.060 |
| High resolution limit [Å] | 1.020 | 1.020 |
| Rmerge | 0.057 | 0.383 |
| Number of reflections | 113536 | |
| <I/σ(I)> | 2.6 | |
| Completeness [%] | 95.5 | 62.6 |
| Redundancy | 6.8 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | Crystal was grown by the hanging-drop vapor-diffusion method at room temperature, from a 2.2 mg/ml protein solution at pH 5.6 with 0.1M MES and 0.6-0.8M sodium chloride. The inhibitor was mixed with protease in a ratio 5:1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
