1VEW
MANGANESE SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU FR-C |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1996-07 |
Detector | RIGAKU |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 100.840, 108.910, 182.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.186 |
Rwork | 0.188 |
R-free | 0.21800 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mng |
RMSD bond length | 0.010 |
RMSD bond angle | 15.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.056 * | 0.191 * |
Total number of observations | 215051 * | |
Number of reflections | 56890 | |
<I/σ(I)> | 22 | 5.4 |
Completeness [%] | 96.8 | 77 |
Redundancy | 3.7 | 0.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | CRYSTALS WERE GROWN AT ROOM TEMPERATURE USING THE HANGING DROP METHOD. THE HANGING DROPS WERE SUSPENDED OVER 0.75ML OF WELL SOLUTION (16-30% PEG6000 AND 0.05M BICINE TITRATED TO PH8.5) AND CONSISTED OF 2UL OF WELL SOLUTION AND 2UL OF PROTEIN SOLUTION (MNSOD AT 12MG/ML IN WATER)., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | drop | PEG6000 | 8-15 (%) | |
3 | 1 | drop | bicine titrated | 0.025 (M) | |
4 | 1 | reservoir | PEG6000 | 16-30 (%) | |
5 | 1 | reservoir | bicine titrated | 0.05 (M) |