2QB2
Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).
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 | 153.910, 84.684, 78.865 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.000 - 1.700 |
| R-factor | 0.14673 |
| Rwork | 0.145 |
| R-free | 0.18419 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1amq |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.832 |
| 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] | 27.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.057 | 0.525 |
| Number of reflections | 54569 | |
| <I/σ(I)> | 13.7 | 2.6 |
| Completeness [%] | 96.1 | 96.6 |
| Redundancy | 4.5 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 298 | The well solutions contained 25 mM potassium phosphate and 43% saturated ammonium sulfate with 20 mM of SADTA at pH 7.0, EVAPORATION, temperature 298K |
