1GN3
H145Q mutant of Mycobacterium tuberculosis iron-superoxide dismutase.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 103.880, 103.880, 69.920 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 4.000 |
| Rwork | 0.168 |
| R-free | 0.18400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ids |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.045 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.000 | |
| High resolution limit [Å] | 4.000 | |
| Rmerge | 0.163 | 0.221 |
| Number of reflections | 5069 | |
| Completeness [%] | 98.4 | |
| Redundancy | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 277 | 100MM TRIS-HCL PH 7.0, 25% PEG 6000, PROTEIN CONCENTRATION = 3 MG/ML, 4 DEGREES CENTIGRADE. |
