1W7M
Crystal structure of human kynurenine aminotransferase I in complex with L-Phe
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Detector | MSC |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 145.672, 145.672, 67.233 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.700 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.23000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w7l |
RMSD bond length | 0.020 |
RMSD bond angle | 1.850 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.700 |
Rmerge | 0.068 * |
Total number of observations | 81664 * |
Number of reflections | 22371 |
Completeness [%] | 98.3 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 4 * | pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | ammonium formate | 4.5 (M) | |
3 | 1 | reservoir | Tris | 0.1 (M) | pH7.5 |