1MAE
The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor
Experimental procedure
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 129.784, 129.784, 104.334 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | ? - 2.800 |
| R-factor | 0.183 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.800 |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| High resolution limit [Å] | 2.800 * | |
| Rmerge | 0.073 * | 0.157 * |
| Total number of observations | 125106 * | |
| Number of reflections | 25377 * | |
| Completeness [%] | 95.7 * | 92.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5 * | 4 * | taken from Ubbink, M. et al (1991). Eur. J. Biochem., 202, 1003-1012. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | sodium acetate | 0.1 (M) | |
| 3 | 1 | reservoir | ammonium sulfate | 37-42 (%sat) | |
| 4 | 1 | reservoir | sodium acetate | 0.1 (M) |






