1NH0
1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-11-12 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 28.913, 66.562, 93.147 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.030 |
R-factor | 0.1305 |
Rwork | 0.130 |
R-free | 0.16540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vik |
RMSD bond length | 0.016 |
RMSD bond angle | 0.036 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | EPMR |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 54.100 | 1.060 |
High resolution limit [Å] | 1.030 | 1.030 |
Rmerge | 0.089 | 0.595 |
Number of reflections | 88784 | |
<I/σ(I)> | 10.5 | 1.85 |
Completeness [%] | 99.0 | 93.3 |
Redundancy | 9.8 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |