1E5X
Structure of threonine synthase from Arabidopsis thaliana
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-10-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 57.760, 62.140, 76.590 |
Unit cell angles | 109.48, 97.61, 112.74 |
Refinement procedure
Resolution | 29.810 - 2.250 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.24300 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 21.900 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.320 |
High resolution limit [Å] | 2.250 * | 2.200 |
Rmerge | 0.033 * | 0.183 * |
Total number of observations | 124846 * | |
Number of reflections | 43719 * | 6265 * |
<I/σ(I)> | 8.9 | 3 |
Completeness [%] | 97.2 | 95.3 |
Redundancy | 2.9 * | 2.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 20 * | 13 % PEG 6000, 1M LICL, MES PH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | 1 (M) | ||
2 | 1 | reservoir | PEG6000 | 13 (%) | |
3 | 1 | reservoir | dithiothreitol | 5 (mM) | |
4 | 1 | reservoir | MES-KOH | ||
5 | 1 | drop | protein | 5 (mg/ml) |