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 |