4WLH
High resolution crystal structure of human kynurenine aminotransferase-I bound to PLP cofactor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-02 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.95369 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 102.440, 107.560, 81.530 |
| Unit cell angles | 90.00, 112.64, 90.00 |
Refinement procedure
| Resolution | 20.980 - 1.280 |
| R-factor | 0.172 |
| Rwork | 0.172 |
| R-free | 0.18700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fvx |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.347 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 75.247 | 1.350 |
| High resolution limit [Å] | 1.280 | 1.280 |
| Rmerge | 0.616 | |
| Number of reflections | 208782 | |
| <I/σ(I)> | 11.4 | 1.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 298 | 29% PEG 4000, 0.2 M sodium acetate, 0.1 M Tris |
