2PB0
Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-05-19 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 96.975, 112.053, 65.553 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.590 - 1.960 |
| R-factor | 0.19936 |
| Rwork | 0.197 |
| R-free | 0.23450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | human Ornithine aminotransferase |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.989 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.102 | 0.494 |
| Number of reflections | 51260 | |
| <I/σ(I)> | 11.9 | 2.7 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 12.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 20% PEG 3350, 0.5M ammonium acetate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
