3ST5
Crystal structure of wild-type HIV-1 protease with C3-Substituted Hexahydrocyclopentafuranyl Urethane as P2-Ligand, GRL-0489A
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 | 2011-02-23 |
| Detector | MAR SCANNER 225 MM PLATE |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.390, 86.552, 45.846 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.450 |
| R-factor | 0.1565 |
| Rwork | 0.157 |
| R-free | 0.21920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nu3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.029 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.500 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.072 | 0.418 |
| Number of reflections | 41487 | |
| <I/σ(I)> | 16 | 2 |
| Completeness [%] | 98.4 | 88.5 |
| Redundancy | 4.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 298 | 1.2 M ammonium chloride, 0.1 M sodium acetate buffer, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
