1PA9
Yersinia Protein-Tyrosine Phosphatase complexed with pNCS (Yop51,Pasteurella X,Ptpase,Yop51delta162) (Catalytic Domain, Residues 163-468) Mutant With Cys 235 Replaced By Arg (C235r)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9A |
| Synchrotron site | NSLS |
| Beamline | X9A |
| Temperature [K] | 140 |
| Detector technology | AREA DETECTOR |
| Collection date | 2002-03-02 |
| Detector | SDMS |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.360, 55.900, 97.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.227 |
| Rwork | 0.226 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ytw |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.290 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.092 * | 0.314 |
| Number of reflections | 17749 | |
| Completeness [%] | 92.5 | 91.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.2 | 4 * | PEG1500, imdazole, pNCS, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 40 (mg/ml) | |
| 2 | 1 | drop | imidazole | 10 (mM) | pH7.2 |
| 3 | 1 | drop | EDTA | 0.2 (mM) | |
| 4 | 1 | drop | beta-mercaptoethanol | 0.1 (%) | |
| 5 | 1 | drop | pNCS inhibitor | 5 (mM) | |
| 6 | 1 | reservoir | imidazole | 20 (mM) | pH7.2 |
| 7 | 1 | reservoir | PEG1500 | 20 (%(w/v)) |
