7N6V
Crystal structure of HIV-1 Protease multiple mutants PRS17 with Revertant mutation V48G bound to inhibitor 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 | PIXEL |
| Collection date | 2020-02-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 61 |
| Unit cell lengths | 62.804, 62.804, 82.450 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.880 - 1.390 |
| R-factor | 0.1623 |
| Rwork | 0.160 |
| R-free | 0.19810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5t2z |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.127 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.440 |
| High resolution limit [Å] | 1.390 | 2.990 | 1.390 |
| Rmerge | 0.086 | 0.075 | 1.114 |
| Rmeas | 0.091 | 0.079 | 1.189 |
| Rpim | 0.029 | 0.025 | 0.409 |
| Total number of observations | 338553 | ||
| Number of reflections | 36885 | 3752 | 3652 |
| <I/σ(I)> | 15.9 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 9.2 | 9.9 | 7.9 |
| CC(1/2) | 0.994 | 0.766 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 298 | 26% PEG 8000, 0.1 M sodium cacodylate pH 6.7, 0.2 M sodium acetate |
