1UN8
Crystal structure of the dihydroxyacetone kinase of C. freundii (native form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 100 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 100.440, 124.590, 237.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 * - 2.500 |
R-factor | 0.2 |
Rwork | 0.196 |
R-free | 0.24500 * |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.432 * |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | |
High resolution limit [Å] | 2.500 | |
Rmerge | 0.066 | 0.361 * |
Number of reflections | 50187 | |
<I/σ(I)> | 14.4 | |
Completeness [%] | 96.8 | 83.7 * |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 | pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30-50 (mg/ml) | |
2 | 1 | drop | HEPES | 5 (mM) | pH7.5 |
3 | 1 | drop | dithiothreitol | 2 (mM) | |
4 | 1 | reservoir | HEPES | 100 (mM) | pH7.3 |
5 | 1 | reservoir | 50 (mM) | ||
6 | 1 | reservoir | PEG3000 | 9 (%(w/v)) | |
7 | 1 | reservoir | glycerol | 25 (%(v/v)) |