1B8P
MALATE DEHYDROGENASE FROM AQUASPIRILLUM ARCTICUM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 59.080, 102.170, 53.790 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.900 |
Rwork | 0.175 |
R-free | 0.17800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.900 |
Rmerge | 0.081 |
Number of reflections | 25856 |
<I/σ(I)> | 24.7 |
Completeness [%] | 97.8 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 18 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 100 (mM) | |
3 | 1 | reservoir | sodium acetate | 400 (mM) | |
4 | 1 | reservoir | PEG4000 | 35 (%) |