2Q05
Crystal structure of tyr/ser protein phosphatase from Vaccinia virus WR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 169.246, 169.246, 169.246 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.570 |
| R-factor | 0.1927 |
| Rwork | 0.191 |
| R-free | 0.21830 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.523 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.660 |
| High resolution limit [Å] | 2.570 | 2.570 |
| Rmerge | 0.133 | 0.899 |
| Number of reflections | 51445 | |
| <I/σ(I)> | 35.5 | 2.21 |
| Completeness [%] | 99.8 | 97.7 |
| Redundancy | 22.5 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 291 | 2M Sodium acetate pH 7.0, B-propane buffer pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
