3QN6
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 | 84.749, 154.678, 79.147 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.229 - 1.790 |
R-factor | 0.1533 |
Rwork | 0.151 |
R-free | 0.18800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.017 |
RMSD bond angle | 1.486 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.15) |
Phasing software | MOLREP |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.574 | 39.574 | 1.840 |
High resolution limit [Å] | 1.790 | 8.010 | 1.790 |
Rmerge | 0.024 | 0.428 | |
Total number of observations | 1410 | 11977 | |
Number of reflections | 48807 | ||
<I/σ(I)> | 10.7 | 26.4 | 1.7 |
Completeness [%] | 99.1 | 79.7 | 99.7 |
Redundancy | 3.4 | 2.9 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 2 L of protein (15-20 mg/ml, 50 mM TEA, pH 7.5, 100 mM KCL, 2 mM DTT, 10 M deaza-PLP) mixed with 2 L reservoir buffer (53-60% saturated ammonium sulfate and 50 mM TEA, pH 7.5), VAPOR DIFFUSION, HANGING DROP, temperature 293K |