4Q1Y
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 | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-11-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9002 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.813, 58.225, 61.824 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.250 - 1.500 |
R-factor | 0.1838 |
Rwork | 0.183 |
R-free | 0.20737 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.497 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.250 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.048 | |
Number of reflections | 29633 | |
<I/σ(I)> | 16.8 | |
Completeness [%] | 98.8 | 96.7 |
Redundancy | 6.5 | 5 |
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 |