1H72
CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 87.990, 87.990, 99.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.800 |
R-factor | 0.177 |
Rwork | 0.177 |
R-free | 0.20700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fwl |
RMSD bond length | 0.016 |
RMSD bond angle | 1.750 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 1.800 | |
Rmerge | 0.089 | |
Total number of observations | 206493 * | |
Number of reflections | 36728 | |
<I/σ(I)> | 21.1 | |
Completeness [%] | 99.8 | 99.9 * |
Redundancy | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.2 * | 100 * | PEG4000, SODIUM ACETATE, pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protease | 15 (mg/ml) | |
2 | 1 | drop | HEPES | 50 (mM) | |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | drop | 5 (mM) | ||
5 | 1 | drop | dithiothreitol | 1 (mM) | |
6 | 1 | drop | substrate | 5 (mM) | |
7 | 1 | reservoir | Tris | 0.1 (M) | |
8 | 1 | reservoir | sodium acetate | 0.2 (M) | |
9 | 1 | reservoir | PEG4000 | 20-25 (%) |