2BB9
Structure of HIV1 protease and AKC4p_133a complex.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2005-01-13 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 58.238, 86.180, 46.533 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.550 - 1.350 |
Rwork | 0.237 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | : 1NPW |
RMSD bond length | 0.013 |
RMSD bond angle | 2.000 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNX (2000.1) |
Refinement software | CNX (2000.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.400 |
High resolution limit [Å] | 1.350 | 1.350 |
Number of reflections | 37834 | |
<I/σ(I)> | 39 | 2.8 |
Completeness [%] | 72.4 | 21 |
Redundancy | 6.1 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 298 | 600MM NACL, 100MM SODIUM ACETATE BUFFER AT PH 5.2, VAPOR DIFFUSION, HANGING DROP , temperature 298K |