2RF6
Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | OXFORD DIFFRACTION ENHANCE ULTRA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-18 |
| Detector | Xcalibur |
| Wavelength(s) | 1.54 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 38.638, 63.994, 135.428 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.950 |
| R-factor | 0.18794 |
| Rwork | 0.187 |
| R-free | 0.20813 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2P4D Variola major H1 phosphatase |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.460 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 6.000 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.054 | 0.169 |
| Number of reflections | 10692 | |
| <I/σ(I)> | 22.4 | 9.4 |
| Completeness [%] | 85.9 | 65.2 |
| Redundancy | 6.6 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH | 7 | 294.15 | 82% PEG 400, 0.1M MOPS pH 7.0, BATCH, temperature 294.15K |
