4F5J
Rational Design and Directed Evolution for Conversion of Substrate Specificity from E.coli Aspartate Aminotransferase to Tyrosine Aminotransferase: Mutant P5.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 85 |
| Detector technology | CCD |
| Collection date | 2010-08-07 |
| Detector | BRUKER SMART 6000 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.706, 102.985, 139.344 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.653 - 1.954 |
| R-factor | 0.1634 |
| Rwork | 0.161 |
| R-free | 0.20360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.065 |
| 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] | 100.000 | 2.050 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.084 | 0.408 |
| Number of reflections | 63086 | |
| <I/σ(I)> | 13.88 | 2.32 |
| Completeness [%] | 99.9 | 99 |
| Redundancy | 5.76 | 3.78 |
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 |
