3EI5
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with PLP-Glu: an external aldimine mimic
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-03-11 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.978483 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 102.556, 102.556, 171.953 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.470 - 2.050 |
R-factor | 0.17303 |
Rwork | 0.170 |
R-free | 0.22078 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2z20 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.640 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.120 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 62726 | |
Completeness [%] | 94.5 | 68.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 45% (NH4)2SO4, 0.1 M HEPES pH 7.5, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298K |