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) |