3KEA
Structure function studies of vaccinia virus host-range protein K1 reveal a novel ankyrin repeat interaction surface for K1s function
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2007-11-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9793453, 0.9794771 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 95.107, 110.263, 86.259 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.280 - 2.300 |
| R-factor | 0.212 |
| Rwork | 0.210 |
| R-free | 0.25400 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.436 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 39.280 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 37088 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 293 | 0.2M Natartrate, 20% PEG3350, 0.1M NaAc, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |






