6U7O
HIV-1 wild type protease with GRL-00819A, with phenyl-boronic-acid as P2'-ligand and with a 6-5-5-ring fused crown-like tetrahydropyranofuran as the P2-ligand
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 | 2019-08-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.921, 86.479, 45.875 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.410 - 1.330 |
| R-factor | 0.1391 |
| Rwork | 0.137 |
| R-free | 0.17720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nu3 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.331 |
| Data reduction software | HKL-2000 (0.716.1) |
| Data scaling software | HKL-2000 (0.716.1) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.380 |
| High resolution limit [Å] | 1.330 | 2.870 | 1.330 |
| Rmerge | 0.061 | 0.045 | 0.749 |
| Rmeas | 0.067 | 0.050 | 0.842 |
| Rpim | 0.027 | 0.020 | 0.376 |
| Total number of observations | 324034 | ||
| Number of reflections | 53993 | 5700 | 5048 |
| <I/σ(I)> | 12.8 | ||
| Completeness [%] | 98.9 | 98.9 | 94.1 |
| Redundancy | 6 | 6.1 | 4.3 |
| CC(1/2) | 0.998 | 0.713 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 1.4 M sodium chloride, 0.1 M sodium acetate buffer pH 6.0 |
