1VSK
ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0
Experimental procedure
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10-31 |
Detector | MAC Science DIP-2000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 67.159, 67.159, 79.651 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.159 |
Rwork | 0.159 |
R-free | 0.24900 |
Starting model (for MR) | 1asv |
RMSD bond length | 0.014 |
RMSD bond angle | 25.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.210 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.077 * | 0.415 * |
Total number of observations | 85055 * | |
Number of reflections | 10132 | |
<I/σ(I)> | 20.7 | 3.6 |
Completeness [%] | 97.0 | 96.5 |
Redundancy | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | Bujacz, G., (1995) J. Mol. Biol., 253, 333. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6-7.5 (mg/ml) | |
2 | 1 | reservoir | HEPES | 100 (mM) | |
3 | 1 | reservoir | isopropanol | 10 (%) | |
4 | 1 | reservoir | PEG4000 | 20 (%) |