3CM3
High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-20 |
| Detector | ADSC Q-270 |
| Wavelength(s) | 0.918 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 63.816, 38.690, 134.987 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.110 - 1.320 |
| R-factor | 0.1717 |
| Rwork | 0.171 |
| R-free | 0.18458 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2rf6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.186 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.370 |
| High resolution limit [Å] | 1.320 | 1.320 |
| Number of reflections | 35905 | |
| <I/σ(I)> | 65.6 | 2.5 |
| Completeness [%] | 90.9 | 51.4 |
| Redundancy | 15.7 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch | 8 | 297 | 62% PEG 400, 0.1M Tris pH 8 , Batch, temperature 297K |
