4DFG
Crystal Structure of Wild-type HIV-1 Protease with Cyclopentyltetrahydro- furanyl Urethanes as P2-ligand, GRL-0249A
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 | 2009-11-18 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | .8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.580, 85.930, 45.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.230 |
| R-factor | 0.1457 |
| Rwork | 0.144 |
| R-free | 0.18010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qci |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.033 |
| 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 | 1.270 |
| High resolution limit [Å] | 1.230 | 1.230 |
| Rmerge | 0.096 | 0.389 |
| Number of reflections | 62205 | |
| <I/σ(I)> | 13.8 | 2 |
| Completeness [%] | 91.3 | 54.7 |
| Redundancy | 5.1 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 298 | The protein concentration was about 4 mg/ml; 1.2 M NaCl and 0.1 M Acetate Buffer pH 4.8, ratio protein:inhibitor 1:5 and 30% glycerol for cyro protection. VAPOR DIFFUSION, HANGING DROP, temperature 298K |
