2E54
Crystal structure of acetylornithine aminotransferase from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-10-16 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 67.222, 115.697, 52.448 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.500 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.21300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vef |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.066 | 0.364 |
| Number of reflections | 66199 | |
| <I/σ(I)> | 14.8 | 5.35 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 8.5 | 295 | 0.2M NaCl, 0.1M Tris-HCl, 25%(w/v) PEG 3350, pH 8.5, microbatch, temperature 295K |
