1OI2
X-ray structure of the dihydroxyacetone kinase from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 100 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 96.509, 97.408, 85.963 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 * - 1.750 |
| R-factor | 0.172 |
| Rwork | 0.172 |
| R-free | 0.20100 |
| Structure solution method | MIR |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.618 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.046 | 0.172 |
| Number of reflections | 78957 | |
| <I/σ(I)> | 19.4 | |
| Completeness [%] | 95.7 | 97.5 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | pH 5.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium acetate | 80 (mM) | pH5.0 |
| 2 | 1 | reservoir | ammonium sulfate | 160 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 17 (%(w/v)) | |
| 4 | 1 | reservoir | MPD | 15 (%(w/v)) | |
| 5 | 1 | drop | protein | 30 (mg/ml) | |
| 6 | 1 | drop | HEPES | 5 (%(w/v)) | pH7.5 |
| 7 | 1 | drop | dithiothreitol | 2 (mM) |
