3EIB
Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-02-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.976067 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 103.045, 103.045, 171.984 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.590 - 1.850 |
R-factor | 0.16401 |
Rwork | 0.162 |
R-free | 0.19749 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2z20 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.344 |
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 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 83053 | |
Completeness [%] | 91.4 | 89.9 |
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 |