4F5L
A Theoretical Optimized Mutant for the Conversion of Substrate Specificity and Activity of Aspartate Aminotransferase to Tyrosine Aminotransferase: Chimera P7.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.736, 102.990, 139.304 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.333 - 1.400 |
| R-factor | 0.1618 |
| Rwork | 0.161 |
| R-free | 0.18080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.133 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 1.440 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.049 | 0.336 |
| Number of reflections | 167317 | |
| <I/σ(I)> | 12.6 | 2.4 |
| Completeness [%] | 98.9 | 90.3 |
| Redundancy | 3.6 | 2.6 |
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 |
