6P9B
HIV-1 Protease multiple drug resistant mutant PRS5B with Amprenavir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-02-17 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 73.663, 73.663, 94.332 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.330 - 1.750 |
R-factor | 0.18366 |
Rwork | 0.182 |
R-free | 0.21731 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nu3 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.897 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.059 | 0.489 |
Rmeas | 0.068 | 0.568 |
Rpim | 0.033 | 0.284 |
Number of reflections | 26189 | 2497 |
<I/σ(I)> | 20.3 | 2.8 |
Completeness [%] | 100.0 | 95 |
Redundancy | 4.1 | 3.7 |
CC(1/2) | 1.000 | 0.820 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | 292 | 1.8 M Ammonium Phosphate and 100 mM Tris buffer at pH 7.9. |