1W7L
Crystal structure of human kynurenine aminotransferase I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 146.372, 146.372, 67.449 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.750 - 2.000 |
| R-factor | 0.193 |
| Rwork | 0.192 |
| R-free | 0.22700 |
| Structure solution method | OTHER |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.170 * |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.051 * |
| Total number of observations | 306700 * |
| Number of reflections | 54768 |
| Completeness [%] | 99.9 |
| Redundancy | 5.6 |
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 |
