1GLL
ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1997-01 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 99.766, 201.148, 114.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.000 |
| Rwork | 0.176 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1glj |
| RMSD bond length | 0.019 |
| RMSD bond angle | 22.495 * |
| Data reduction software | SDMS |
| Data scaling software | SDMS |
| Refinement software | TNT (5F) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 3.000 |
| Rmerge | 0.068 |
| Total number of observations | 53041 * |
| Number of reflections | 20445 * |
| Completeness [%] | 83.0 |
| Redundancy | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | pH 6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 5 (mg/ml) | |
| 2 | 1 | drop | PEG1000 | 8.3 (%) | |
| 3 | 1 | drop | 0.13 (M) | ||
| 4 | 1 | drop | PIPES | 0.04 (M) | |
| 5 | 1 | drop | 0.08 (M) | ||
| 6 | 1 | drop | inhibitor | 8.3 (mM) | |
| 7 | 1 | reservoir | PEG1000 | 20 (%) | |
| 8 | 1 | reservoir | 0.3 (M) | ||
| 9 | 1 | reservoir | PIPES | 0.1 (M) |
