4HLA
Crystal structure of wild type HIV-1 protease in complex with darunavir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2012-09-25 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.54 |
Spacegroup name | P 61 |
Unit cell lengths | 62.150, 62.150, 82.191 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.790 - 1.950 |
R-factor | 0.19354 |
Rwork | 0.192 |
R-free | 0.22779 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.456 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 29.070 |
High resolution limit [Å] | 1.950 |
Rmerge | 0.069 |
Number of reflections | 13144 |
Redundancy | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 1.6 M Ammonium sulfate, 0.1 M MES monohydrate (pH 6.0), VAPOR DIFFUSION, HANGING DROP, temperature 298K |