1XXP
Yersinia YopH (residues 163-468) C403S binds phosphotyrosyl peptide at two sites
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Detector | UCSD MARK III |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 54.170, 71.090, 47.860 |
| Unit cell angles | 111.80, 90.00, 109.70 |
Refinement procedure
| Resolution | 20.000 - 3.000 |
| Rwork | 0.181 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yts |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.177 |
| Data reduction software | SDMS |
| Data scaling software | SDMS |
| Phasing software | X-PLOR |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 3.000 |
| Rmerge | 0.118 |
| Number of reflections | 10084 |
| Completeness [%] | 86.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 10-12 mg/ml protein + 1 mM phosphopeptide. Precipitant: 18-24% polyethylene glycol (PEG) 8000, 50-100 mM NaCl, 0.1% beta-mercaptoethanol, 100 mM TrisCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
