3QAA
HIV-1 wild type protease with a substituted bis-Tetrahydrofuran inhibitor, GRL-044-10A
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 | IMAGE PLATE |
| Collection date | 2010-11-17 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.435, 86.112, 46.032 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.400 |
| R-factor | 0.1717 |
| Rwork | 0.172 |
| R-free | 0.22950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qci |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.029 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.080 | 0.597 |
| Number of reflections | 45049 | |
| <I/σ(I)> | 13.9 | 2.1 |
| Completeness [%] | 96.6 | 87.1 |
| Redundancy | 6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | pH 5.5, 0.1 M Sodium Citrate, 1.2 M Sodium Chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
