3VF5
Crystal Structure of HIV-1 Protease Mutant I47V with novel P1'-Ligands GRL-02031
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 | CCD |
| Collection date | 2009-02-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.203, 86.394, 45.946 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.250 |
| R-factor | 0.1468 |
| R-free | 0.16860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h5b |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.033 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 1.290 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.068 | 0.326 |
| Number of reflections | 61338 | |
| <I/σ(I)> | 19.9 | 2.4 |
| Completeness [%] | 94.6 | 63.7 |
| Redundancy | 6.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.2 | 298 | NaCl/sodium acetate buffer at pH 4.2 The concentration of protein is around 1.5-1.6 mg/ml The ratio for protein/inhibitor is 1:5., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
