1VSH
ASV INTEGRASE CORE DOMAIN WITH ZN(II) COFACTORS
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1996-07-22 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 66.080, 66.080, 80.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.950 |
R-factor | 0.173 * |
Rwork | 0.173 |
Structure solution method | ISOSTRUCTURAL TO PDB ENTRY 1VSF |
RMSD bond length | 0.013 |
RMSD bond angle | 0.043 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | PROFFT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 13238 | |
<I/σ(I)> | 13.4 | 2.6 |
Completeness [%] | 97.0 | 94.7 |
Redundancy | 3.7 | 3.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 4000, 10% ISOPROPANOL, 100 MM HEPES, PH 7.5, THEN SOAKED IN 100 MM ZNCL2. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
2 | 1 | reservoir | HEPES | 100 (mM) | |
3 | 1 | reservoir | isopropanol | 10 (%) | |
4 | 1 | drop | protein | 6-7.5 (mg/ml) |