3QPG
Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Detector technology | CCD |
Detector | MARMOSAIC 325 mm CCD |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 83.785, 154.834, 77.799 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.500 - 1.790 |
R-factor | 0.149 |
Rwork | 0.148 |
R-free | 0.17900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.518 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.500 |
High resolution limit [Å] | 1.790 |
Number of reflections | 46701 |
<I/σ(I)> | 17.5 |
Completeness [%] | 98.2 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 293 | 2 uL of protein solution(15-20 mg/ml, 50 mM TEA, pH 7.5, 100 mM KCL, 2 mM DTT, 10 mM deaza-PLP, 50 mM L-aspartate) mixed with 2 uL reservoir buffer (53-60% saturated ammonium sulfate and 50 mM TEA, pH 7.5), VAPOR DIFFUSION, HANGING DROP, temperature 293K |