4F5H
Intercoversion of Substrate Specificity: E. coli Aspatate Aminotransferase to Tyrosine Aminotransferase: Chimera P3.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.129, 109.785, 141.673 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.955 - 1.600 |
| R-factor | 0.1624 |
| Rwork | 0.161 |
| R-free | 0.18690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.083 |
| 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] | 50.000 | 1.640 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.052 | 0.367 |
| Number of reflections | 118914 | |
| <I/σ(I)> | 9.9 | 2.6 |
| Completeness [%] | 99.1 | 98.6 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 277 | 8% PEG 4000, 0.1 M Sodium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
