3NU4
Crystal Structure of HIV-1 Protease Mutant V32I with Antiviral Drug Amprenavir
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 | 2007-03-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 57.769, 86.130, 46.284 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.200 |
| R-factor | 0.1619 |
| Rwork | 0.162 |
| R-free | 0.20020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nu3 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.031 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.240 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.081 | 0.442 |
| Number of reflections | 66626 | |
| <I/σ(I)> | 2.5 | |
| Completeness [%] | 91.6 | 62.7 |
| Redundancy | 6.1 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 298 | The vapour diffusion, hanging drop method is applied. Amprenvir was dissolved in DMSO. Protein concentration is 2.2 mg/ml. The ratio of inhibitor to protein is 5:1 in 0.1 M sodium acetate buffer (ph=5.4), with 0.4M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
