1EBK
Structural and kinetic analysis of drug resistant mutants of HIV-1 protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.410, 61.950, 51.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.060 |
Rwork | 0.192 |
R-free | 0.30600 |
RMSD bond length | 0.013 * |
RMSD bond angle | 1.990 * |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Rmerge | 0.084 |
Number of reflections | 19007 |
Completeness [%] | 79.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 298 | CITRATE/PHOSPHATE BUFFER 0.05M, DTT 10MM, DMSO 10%, SATURATED AMMONIUM SULPHATE (25-50%), PROTEIN 2-5 MG/ML, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protease | 4.5-8.0 (mg/ml) | |
2 | 1 | drop | sodium acetate | 20-55 (mM) | |
3 | 1 | reservoir | sodium citrate | 66 (mM) | |
4 | 1 | reservoir | sodium phosphate | 132 (mM) | |
5 | 1 | reservoir | ammonium sulfate | 30-36 (%sat) |