3OXV
Crystal Structure of HIV-1 I50V, A71 Protease in Complex with the protease inhibitor amprenavir.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.03 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.563, 63.338, 58.613 |
| Unit cell angles | 90.00, 96.61, 90.00 |
Refinement procedure
| Resolution | 31.320 - 1.750 |
| R-factor | 0.1705 |
| Rwork | 0.169 |
| R-free | 0.20540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f7a |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.360 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.070 | 0.027 | 0.441 |
| Number of reflections | 36283 | ||
| <I/σ(I)> | 8.7 | ||
| Completeness [%] | 98.0 | 97.8 | 97 |
| Redundancy | 4.1 | 3.9 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 295 | 126mM Phosphate buffer pH 6.2, 63mM Sodium Citrate, 18-33% Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
