4Q1W
Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-09-18 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.741, 57.550, 61.809 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.220 - 1.850 |
R-factor | 0.17454 |
Rwork | 0.173 |
R-free | 0.20634 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.342 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.220 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.064 | |
Number of reflections | 15822 | |
<I/σ(I)> | 19.3 | |
Completeness [%] | 98.6 | 95.2 |
Redundancy | 6.8 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 295 | 126mM Phosphate buffer, 63mM Sodium Citrate, 24-29% Ammonium Sulfate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K |