2CDQ
Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-12-15 |
Detector | MARRESEARCH |
Spacegroup name | I 41 |
Unit cell lengths | 117.342, 117.342, 255.283 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.670 - 2.850 |
R-factor | 0.204 |
Rwork | 0.202 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.121 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.000 |
High resolution limit [Å] | 2.850 | 2.850 |
Rmerge | 0.072 | 0.440 |
Number of reflections | 38693 | |
<I/σ(I)> | 8.3 | 1.7 |
Completeness [%] | 96.6 | 98.1 |
Redundancy | 3.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.2 M DI-SODIUM TARTRATE DIHYDRATE, 20 % PEG 3350, pH 6.50 |