1N0J
The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles
Replaces: 1ABMExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Detector | SIEMENS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 76.130, 79.900, 68.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.200 |
R-factor | 0.171 |
Rwork | 0.171 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.018 |
RMSD bond angle | 3.300 |
Data reduction software | X-GEN |
Refinement software | X-PLOR (20) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.090 | |
Total number of observations | 117362 * | |
Number of reflections | 19738 | |
Completeness [%] | 92.0 | 52 |
Redundancy | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.8 * | 293 | peg 600, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | phosphate | 50 (mM) | pH7.8 |
3 | 1 | reservoir | PEG400 | 24-30 (%) |