1LV1
Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200HB |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 2001-01-01 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 |
Unit cell lengths | 63.060, 63.060, 83.420 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 * - 2.100 |
R-factor | 0.1935 * |
Rwork | 0.194 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 26.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.071 | |
Total number of observations | 51200 * | |
Number of reflections | 10245 * | |
<I/σ(I)> | 10.1 | |
Completeness [%] | 93.1 | 85 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 295 | 5% saturated ammonium sulfate, 200mM sodium phosphate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | sodium acetate | 50 (mM) | |
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | reservoir | ammonium sulfate | 5 (%sat) | |
5 | 1 | reservoir | sodium phosphate | 200 (mM) | |
6 | 1 | reservoir | sodium citrate | 100 (mM) | pH6.2 |