7N6X
Crystal structure of HIV-1 Protease multiple mutants PRS17 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 | 2018-10-25 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 61 |
| Unit cell lengths | 62.994, 62.994, 82.691 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.970 - 1.470 |
| R-factor | 0.2006 |
| Rwork | 0.199 |
| R-free | 0.22720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5t2z |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.396 |
| Data reduction software | HKL-2000 (0.719.2) |
| Data scaling software | HKL-2000 (0.719.2) |
| 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 | 1.520 |
| High resolution limit [Å] | 1.470 | 3.170 | 1.470 |
| Rmerge | 0.063 | 0.051 | 1.124 |
| Rmeas | 0.066 | 0.054 | 1.198 |
| Rpim | 0.021 | 0.017 | 0.406 |
| Total number of observations | 306763 | ||
| Number of reflections | 31170 | 3176 | 3010 |
| <I/σ(I)> | 21.5 | ||
| Completeness [%] | 98.6 | 98.6 | 95.7 |
| Redundancy | 9.8 | 10.1 | 8.2 |
| CC(1/2) | 0.996 | 0.664 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 37.5% Tacsimate (Hampton Research) |
