2AQU
Structure of HIV-1 protease bound to atazanavir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-07-18 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.1 |
Spacegroup name | P 61 |
Unit cell lengths | 62.411, 62.411, 82.569 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.830 - 2.000 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.23800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1sgu |
RMSD bond length | 0.021 |
RMSD bond angle | 2.300 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.472 | |
Number of reflections | 12320 | |
<I/σ(I)> | 2.5 | |
Completeness [%] | 81.0 | 88.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.5 | 298 | 0.17M Ammonium Sulfate, 0.085M Sodium Cacodylate, 25.5% PEG 8000, 15% v/v Glycerol anhydrous, pH 6.5, EVAPORATION, temperature 298 K |