1VEF
Acetylornithine aminotransferase from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-03-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.820, 70.959, 92.083 |
| Unit cell angles | 90.00, 107.60, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.350 |
| R-factor | 0.195 |
| Rwork | 0.195 |
| R-free | 0.20900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oat |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 99.000 |
| High resolution limit [Å] | 1.350 |
| Rmerge | 0.058 |
| Number of reflections | 162897 |
| Completeness [%] | 96.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | PEG8000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
