8DCI
Crystal Structure of a highly resistant HIV-1 protease Clinical isolate PR10x (inhibitor-free)
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 | 2018-04-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 28.366, 81.351, 85.615 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.500 - 1.620 |
| R-factor | 0.1904 |
| Rwork | 0.189 |
| R-free | 0.22650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7L3S |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.714 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.680 |
| High resolution limit [Å] | 1.620 | 3.490 | 1.620 |
| Rmerge | 0.075 | 0.054 | 0.476 |
| Rmeas | 0.082 | 0.059 | 0.528 |
| Rpim | 0.034 | 0.025 | 0.224 |
| Total number of observations | 148165 | ||
| Number of reflections | 25357 | 2705 | 2417 |
| <I/σ(I)> | 16.5 | ||
| Completeness [%] | 97.9 | 96.5 | 95 |
| Redundancy | 5.8 | 5.3 | 5.3 |
| CC(1/2) | 0.996 | 0.895 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 298 | Hanging-drop vapor diffusion using equal volumes of protein stock (3.9 mg/mL) and well reservoir solution. Cryoprotected in 30% glycerol. Crystallized in 0.85 M NaCl and 0.1 M sodium acetate pH 5.4 |
