4NPU
Crystal Structure of HIV-1 Protease Multiple Mutant P51
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-29 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 |
Unit cell lengths | 46.685, 46.685, 101.617 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.640 - 1.500 |
R-factor | 0.1609 |
Rwork | 0.159 |
R-free | 0.19744 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3uf3 |
RMSD bond length | 0.023 |
RMSD bond angle | 2.070 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.067 | 0.277 |
Number of reflections | 34414 | |
<I/σ(I)> | 23.2 | 4.6 |
Completeness [%] | 99.4 | 95.5 |
Redundancy | 8 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.1 M imidazole, 1.0 M sodium acetate trihydrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |