1SH9
Comparing the Accumulation of Active Site and Non-active Site Mutations in the HIV-1 Protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 298 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 |
Unit cell lengths | 62.121, 62.121, 84.784 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.770 - 2.500 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hxw |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.770 | 2.590 |
High resolution limit [Å] | 2.480 | 2.480 |
Number of reflections | 6598 | |
<I/σ(I)> | 4.4 | |
Completeness [%] | 97.8 | 89.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 298 | 20mM Sodium Acetate, 1.5 M Ammonium Sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.00 |