3ATH
Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with four AKGs as substrates and allosteric effectors
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-24 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 85.817, 70.989, 136.816 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.350 - 1.690 |
| R-factor | 0.17185 |
| Rwork | 0.170 |
| R-free | 0.21449 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3aov |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.327 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.750 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.052 | 0.457 |
| Number of reflections | 91289 | |
| <I/σ(I)> | 26.015 | 2.742 |
| Completeness [%] | 99.2 | 99.9 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 20% (w/v) PEG 1000, 0.1M imidazole pH8.0, 0.2M calcium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
