1ETV
THE CRYSTAL STRUCTURE OF E. COLI FIS MUTANT G72A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10-14 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.290, 50.370, 47.260 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.570 - 2.000 |
Rwork | 0.223 |
R-free | 0.26300 |
Starting model (for MR) | The wild-type FIS |
RMSD bond length | 0.008 |
RMSD bond angle | 18.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.074 * | 0.436 * |
Total number of observations | 61673 * | |
Number of reflections | 13105 | |
<I/σ(I)> | 23.3 | |
Completeness [%] | 99.3 | 99.2 |
Redundancy | 4.71 | 4.57 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 15 mg/ml protein, 0.5 M sodium chloride, 0.05 M Na-Hepes (pH 7.5), 15% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | 1 (M) | ||
3 | 1 | drop | Tris-HCl | 20 (mM) | |
4 | 1 | reservoir | Na-HEPES | 0.1 (M) | |
5 | 1 | reservoir | PEG4000 | 30 (%) |