1VSM
ASV INTEGRASE CORE DOMAIN IN CITRATE BUFFER PH 5.0
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-01-09 |
| Detector | MACSCIENCE |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.091, 67.091, 79.237 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.150 |
| R-factor | 0.146 |
| Rwork | 0.146 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1asv |
| RMSD bond length | 0.013 |
| RMSD bond angle | 24.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.190 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.080 * | |
| Total number of observations | 28268 * | |
| Number of reflections | 9166 | |
| <I/σ(I)> | 3 | 10 |
| Completeness [%] | 85.7 | 86.5 |
| Redundancy | 3 |
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 (%) |
