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 |