2Q7W
Structural Studies Reveals the Inactivation of E. coli L-aspartate aminotransferase (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via two mechanisms at pH 6.0
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-02-20 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 153.623, 85.135, 78.849 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 76.920 - 1.400 |
| R-factor | 0.15556 |
| Rwork | 0.154 |
| R-free | 0.18836 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1amq |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.923 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 77.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.062 | 0.571 |
| Number of reflections | 93239 | |
| <I/σ(I)> | 17.4 | 2.7 |
| Completeness [%] | 97.0 | 99.8 |
| Redundancy | 5.7 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6 | 298 | 25 mM potassium phosphate, 43% saturated ammonium sulfate, 20 mM SADTA, pH 6.0, EVAPORATION, temperature 298K |
