3VFB
Crystal Structure of HIV-1 Protease Mutant N88D 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 | 2009-03-27 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.255, 86.386, 46.068 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.550 |
| R-factor | 0.1578 |
| R-free | 0.21560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h5b |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.028 |
| 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] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.075 | 0.425 |
| Number of reflections | 34554 | |
| <I/σ(I)> | 23.2 | 4.2 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 7.1 | 6.3 |
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 no higher than 3 mg/ml. The ratio for protein/inhibitor is 1:5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
