4F5F
Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 85 |
| Detector technology | CCD |
| Collection date | 2010-08-18 |
| Detector | BRUKER SMART 6000 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.189, 103.685, 138.904 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 57.703 - 2.250 |
| R-factor | 0.1761 |
| Rwork | 0.174 |
| R-free | 0.21330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.045 |
| Data reduction software | PROTEUM PLUS (PLUS) |
| Data scaling software | PROTEUM PLUS (PLUS) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.703 | 2.340 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.087 | 0.325 |
| Number of reflections | 41556 | |
| <I/σ(I)> | 12.83 | 2.53 |
| Completeness [%] | 98.6 | 87.5 |
| Redundancy | 4.91 | 2.35 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | 8% PEG 4000, 0.1 M Sodium Acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |






