1KA8
Crystal Structure of the Phage P4 Origin-Binding Domain
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-16 |
Wavelength(s) | 0.9794, 0.9795, 0.9537 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 82.549, 82.549, 232.629 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 * - 2.950 |
R-factor | 0.237 * |
Rwork | 0.241 |
R-free | 0.28400 |
Structure solution method | MAD |
RMSD bond length | 0.013 |
RMSD bond angle | 22.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | 3.060 |
High resolution limit [Å] | 2.950 * | 2.950 |
Rmerge | 0.070 * | |
Completeness [%] | 99.0 * | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293 | used macroseeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium citrate | 100 (mM) | pH4.5-5.0 |
2 | 1 | reservoir | ammonium sulfate | 1.5-1.7 (M) | |
3 | 1 | drop | protein | 12 (mg/ml) |