2QBT
Structural Studies Reveal The Inactivation of E. coli L-aspartate aminotransferase by (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 8.0)
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 | 154.149, 84.760, 78.951 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.800 - 1.750 |
| R-factor | 0.15093 |
| Rwork | 0.149 |
| R-free | 0.19031 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1amq |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.486 |
| 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] | 24.800 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.065 | 0.589 |
| Number of reflections | 48869 | |
| <I/σ(I)> | 12.5 | 2.3 |
| Completeness [%] | 98.2 | 99.5 |
| Redundancy | 4.7 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 8 | 298 | 25 mM potassium phosphate, 43% saturated ammonium sulfate, 20 mM SADTA, pH 8.0, EVAPORATION, temperature 298K |
