5JFU
HIV-1 wild Type protease with GRL-007-14A (a Adamantane P1-Ligand with bis-THF in P2 and benzylamine in P1')
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.958, 86.378, 45.918 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.700 |
| R-factor | 0.2278 |
| Rwork | 0.225 |
| R-free | 0.27820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nu3 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.022 |
| Data reduction software | HKL-2000 (98.705a) |
| Data scaling software | HKL-2000 (98.705a) |
| Phasing software | PHASER |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.076 | 0.487 |
| Number of reflections | 26464 | |
| <I/σ(I)> | 19 | 2.96 |
| Completeness [%] | 99.9 | 99.7 |
| Redundancy | 5.9 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 1.15 M LiCl, 0.1 M Acetate, pH 5.5 |
