1UMW
Structure of a human Plk1 Polo-box domain/phosphopeptide complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX14.1 |
Synchrotron site | SRS |
Beamline | PX14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.352, 79.518, 61.993 |
Unit cell angles | 90.00, 93.26, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.900 |
R-factor | 0.229 |
Rwork | 0.230 |
R-free | 0.25800 * |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.920 |
High resolution limit [Å] | 1.900 * | 1.850 |
Rmerge | 0.053 | 0.530 |
Number of reflections | 50058 | |
<I/σ(I)> | 20 | 2.6 |
Completeness [%] | 97.7 | 97.1 |
Redundancy | 3.6 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8 | 18 * | pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | peptide | 0.2 (mM) | |
2 | 1 | 1 | Tris-HCl | 20 (mM) | pH8.0 |
3 | 1 | 1 | 500 (mM) | ||
4 | 1 | 1 | EDTA | 1 (mM) | |
5 | 1 | 1 | dithiothreitol | 3 (mM) |