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 |