1NH0
1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-12 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 28.913, 66.562, 93.147 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.030 |
| R-factor | 0.1305 |
| Rwork | 0.130 |
| R-free | 0.16540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vik |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.036 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | EPMR |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.100 | 1.060 |
| High resolution limit [Å] | 1.030 | 1.030 |
| Rmerge | 0.089 | 0.595 |
| Number of reflections | 88784 | |
| <I/σ(I)> | 10.5 | 1.85 |
| Completeness [%] | 99.0 | 93.3 |
| Redundancy | 9.8 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
