1GLF
CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1990-08-01 |
| Detector | SDMS |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 92.100, 117.400, 108.400 |
| Unit cell angles | 90.00, 93.10, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.620 |
| R-factor | 0.146 * |
| Rwork | 0.146 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gla |
| RMSD bond length | 0.020 |
| RMSD bond angle | 20.904 * |
| Data reduction software | SDMS |
| Data scaling software | SDMS |
| Phasing software | FRFSUM ((WOLFGANG KABSCH)) |
| Refinement software | TNT (5F-6) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.620 |
| Rmerge | 0.076 |
| Total number of observations | 190143 * |
| Number of reflections | 58942 |
| Completeness [%] | 84.0 |
| Redundancy | 3.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | Faber, H.R., (1989) J. Mol. Biol., 207, 637. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-30 (mg/ml) | |
| 2 | 1 | drop | sodium potassium phosphate | 50 (mM) | |
| 3 | 1 | drop | glycerol | 10 (mM) | |
| 4 | 1 | drop | beta-mercaptoethanol | 2 (mM) | |
| 5 | 1 | reservoir | 300-500 (mM) | ||
| 6 | 1 | reservoir | PEG1550 | 20 (%(w/w)) | PEG1550 to 20000 |
| 7 | 1 | reservoir | sodium potassium phosphate | 50 (mM) | |
| 8 | 1 | drop | ADP | 100 (mM) |
