1ZSR
Crystal structure of wild type HIV-1 protease (BRU isolate) with a hydroxyethylamine peptidomimetic inhibitor BOC-PHE-PSI[S-CH(OH)CH2NH]-PHE-GLU-PHE-NH2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-04-10 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 61 |
| Unit cell lengths | 62.801, 62.801, 82.222 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.000 - 2.060 |
| R-factor | 0.1936 |
| Rwork | 0.202 |
| R-free | 0.28420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1iiq |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.650 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.110 |
| High resolution limit [Å] | 2.060 | 2.060 |
| Rmerge | 0.075 | 0.305 |
| Number of reflections | 10981 | |
| <I/σ(I)> | 26.7 | 4.98 |
| Completeness [%] | 97.6 | 69.8 |
| Redundancy | 6.98 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.3 | 280 | 1 M Ammonium Phosphate, 0.1 M Na Citrate, 3 mg/ml protein, pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 280K |
