3PY9
X-ray structural studies of the entire extra-cellular region of the Ser/Thr kinase PrkC from Staphylococcus aureus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-30 |
| Detector | RIGAKU SATURN 92 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 55.681, 69.103, 88.430 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 9.970 - 2.200 |
| R-factor | 0.24674 |
| Rwork | 0.244 |
| R-free | 0.29346 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.286 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | Auto-Rickshaw |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.080 | |
| Number of reflections | 18045 | |
| Completeness [%] | 99.9 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 5 mg/mL protein solution, 21% (w/v) MPEG2000, 3% w/v D-(+)-galactose, 160 mM ammonium sulfate and 60 mM sodium acetate trihydrate buffer, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
