1MNG
STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS
Experimental procedure
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 146.800, 146.800, 55.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.179 |
| Rwork | 0.179 |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.984 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 * |
| High resolution limit [Å] | 1.800 * |
| Rmerge | 0.077 * |
| Number of reflections | 52673 * |
| Redundancy | 6.5 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 4 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-10 (mg/ml) | |
| 2 | 1 | drop | phosphate | 5 (mM) | |
| 3 | 1 | drop | ammonium sulfate | ||
| 4 | 1 | reservoir | ammonium sulfate | 40 (%sat) | |
| 5 | 1 | reservoir | potassium acid phosphate | 0.5 (M) |






