3A2O
Crystal Structure of HIV-1 Protease Complexed with KNI-1689
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-06 |
Wavelength(s) | 0.800 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 58.223, 85.815, 46.484 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 0.880 |
R-factor | 0.101 |
Rwork | 0.101 |
R-free | 0.11800 |
Structure solution method | FOURIER SYNTHESIS |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 0.910 |
High resolution limit [Å] | 0.880 | 0.880 |
Rmerge | 0.071 | 0.335 |
Number of reflections | 169767 | |
<I/σ(I)> | 2.5 | |
Completeness [%] | 92.2 | |
Redundancy | 8.4 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 126mM phosphate, 63mM sodium citrate buffer pH 5.0, 0.2M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |