1BO5
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 102 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-05-15 |
| Detector | RIGAKU RAXIS II |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 169.410, 169.410, 204.676 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.200 |
| Rwork | 0.211 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gla |
| RMSD bond length | 0.016 |
| RMSD bond angle | 20.924 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | TNT (5F) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 3.200 |
| Rmerge | 0.092 |
| Total number of observations | 188539 * |
| Number of reflections | 54096 |
| Completeness [%] | 94.0 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | glycerol | 10 (mM) | |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | beta-mercaptoethanol | 2 (mM) | |
| 5 | 1 | drop | HEPES | 20 (mM) | |
| 6 | 1 | reservoir | sodium citrate | 1 (M) | |
| 7 | 1 | reservoir | HEPES | 0.1 (M) | |
| 8 | 1 | reservoir | beta-mercaptoethanol | 1 (mM) |
