1ETO
THE CRYSTAL STRUCTURE OF E. COLI FIS MUTANT R71L
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-16 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.030, 70.830, 74.690 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.960 - 1.900 |
Rwork | 0.225 |
R-free | 0.26000 |
Starting model (for MR) | The wild-type FIS |
RMSD bond length | 0.011 |
RMSD bond angle | 20.000 * |
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 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.057 * | 0.511 * |
Total number of observations | 114334 * | |
Number of reflections | 19893 | |
<I/σ(I)> | 30.7 | |
Completeness [%] | 99.8 | 100 |
Redundancy | 5.75 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 10 mg/ml protein, 0.5 M sodium chloride, 0.05 M Na-Hepes (pH 7.5), 1.0 M ammonium sulfate, 1% PEG 400, 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 | ammonium sulfate | 2.0 (M) | |
5 | 1 | reservoir | PEG400 | 2 (%) |