2Z20
Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-11-26 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793, 0.9795, 0.9185 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 102.909, 102.909, 171.452 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.950 |
R-factor | 0.18387 |
Rwork | 0.182 |
R-free | 0.22713 |
Structure solution method | MAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.679 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 72271 | |
<I/σ(I)> | 15.4 | 2.3 |
Completeness [%] | 93.6 | 94.4 |
Redundancy | 6.2 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 45% (NH4)2SO4, 0.1M HEPES pH7.5, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |