4Q1X
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 | 2008-09-22 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.906, 58.277, 61.775 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.410 - 1.900 |
| R-factor | 0.18289 |
| Rwork | 0.180 |
| R-free | 0.23410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.474 |
| 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] | 42.410 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.063 | |
| Number of reflections | 14168 | |
| <I/σ(I)> | 15.2 | |
| Completeness [%] | 93.9 | 91.4 |
| Redundancy | 7.1 | 7.1 |
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 |
