1BDM
THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.750, 88.640, 118.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | ? - 1.800 |
| R-factor | 0.169 |
| Rwork | 0.169 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.770 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Rmerge | 0.071 * |
| Total number of observations | 376446 * |
| Number of reflections | 63904 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 13-15 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 3 | 1 | reservoir | PEG3350 | 20-24 (%) | |
| 4 | 1 | reservoir | 200-800 (mM) | ||
| 5 | 1 | reservoir | oxaloacetate | 20 (mM) | |
| 6 | 1 | reservoir | NADH | 0.2-0.5 (mM) |
