1O9O
Crystal structure of the S131A mutant of Malonamidase E2 complexed with malonamate from Bradyrhizobium japonicum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 103.770, 95.138, 75.057 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.166 |
Rwork | 0.166 |
R-free | 0.23500 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1GR8 |
RMSD bond length | 0.003 * |
RMSD bond angle | 0.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.086 * | 0.231 * |
Total number of observations | 345190 * | |
Number of reflections | 33684 | |
<I/σ(I)> | 9.6 | 2.83 |
Completeness [%] | 90.1 | 79.8 |
Redundancy | 3 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 | 20% PEG1000, 0.1M TRIS-HCL PH7.0, 5MM MALONAMATE, pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG1000 | 20 (%) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH7.0 |