2QB3
Structural Studies Reveal the Inactivation of E. coli L-Aspartate Aminotransferase by (s)-4,5-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 7.5)
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 | 153.316, 85.145, 78.833 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.800 - 1.450 |
| R-factor | 0.14424 |
| Rwork | 0.142 |
| R-free | 0.17774 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.903 |
| 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 | 1.500 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.056 | 0.516 |
| Number of reflections | 169762 | |
| <I/σ(I)> | 14.5 | 3.6 |
| Completeness [%] | 97.1 | 97.3 |
| Redundancy | 6.5 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.5 | 298 | The well solutions contained 25 mM potassium phosphate and 43% saturated ammonium sulfate with 20 mM of SADTA at pH 7.5, EVAPORATION, temperature 298K |
