1XXV
Yersinia YopH (residues 163-468) binds phosphonodifluoromethyl-Phe containing hexapeptide at two sites
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Detector | UCSD MARK III |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 54.130, 47.170, 71.820 |
Unit cell angles | 104.45, 115.05, 89.97 |
Refinement procedure
Resolution | 50.000 - 2.500 |
Rwork | 0.178 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | YopH (residues 163-468) with bound VO4 (not submitted to PDB) |
RMSD bond length | 0.007 |
RMSD bond angle | 1.183 |
Data reduction software | SDMS |
Data scaling software | SDMS |
Phasing software | MERLOT |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.500 |
Rmerge | 0.075 |
Number of reflections | 18319 |
Completeness [%] | 85.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 10 mg/ml protein, 0.5 mM phosphonodifluoro-Phe-containing peptide in 1 mM imidazole. Precipitant: 22% polyethylene glycol (PEG) 4000, 8 mM MnCl2, 0.1% beta-mercaptoethanol, 100 mM Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |