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 |