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CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE
Experimental procedure
| Spacegroup name | P 32 |
| Unit cell lengths | 71.530, 71.530, 107.480 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.000 - 2.500 |
| R-factor | 0.168 |
| Rwork | 0.168 |
| R-free | 0.22200 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.930 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.500 * |
| Rmerge | 0.059 * |
| Number of reflections | 19476 |
| Completeness [%] | 91.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | beta-mercaptoethanol | 0.1 (%) | |
| 3 | 1 | drop | imidazole | 1 (mM) | |
| 4 | 1 | drop | PEG1500 | 10-15 (%) | |
| 5 | 1 | reservoir | PEG1500 | 30 (%) | |
| 6 | 1 | drop | MPD | small amount |
