1NHP
CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303
Experimental procedure
Spacegroup name | I 2 2 2 |
Unit cell lengths | 77.600, 134.800, 146.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.176 |
Rwork | 0.176 |
RMSD bond length | 0.011 * |
RMSD bond angle | 2.600 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
High resolution limit [Å] | 2.000 * | 2.040 * |
Rmerge | 0.042 * | |
Number of reflections | 49100 | |
Completeness [%] | 90.6 | 74.2 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 25 (mM) | |
3 | 1 | drop | EDTA | 0.3 (mM) | |
4 | 1 | drop | dithiothreitol | 2 (mM) | |
5 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
6 | 1 | reservoir | FAD | 0.005 (mM) | |
7 | 1 | reservoir | potassium phosphate | 100 (mM) |