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. |