1BMD
DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.510, 87.590, 118.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | ? - 1.900 |
R-factor | 0.154 |
Rwork | 0.154 |
RMSD bond length | 0.016 |
RMSD bond angle | 2.850 |
Phasing software | X-PLOR |
Refinement software | TNT |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.900 * |
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 | reservoir | protein | 13-15 (mg/ml) | |
2 | 1 | reservoir | Tris | 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) |