1P22
Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity on the SCFbeta-TrCP1 ubiquitin ligase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 103 |
Detector technology | CCD |
Collection date | 2001-12-23 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9500 |
Spacegroup name | P 31 |
Unit cell lengths | 82.600, 82.600, 111.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.950 |
R-factor | 0.23315 |
Rwork | 0.230 |
R-free | 0.28600 * |
Structure solution method | MAD |
RMSD bond length | 0.014 * |
RMSD bond angle | 1.855 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | DM |
Refinement software | REFMAC (5.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.025 |
High resolution limit [Å] | 2.950 | 2.950 |
Rmerge | 0.040 * | 0.430 * |
Total number of observations | 52111 * | |
Number of reflections | 17628 | |
Completeness [%] | 99.3 | 99.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 298 | PEG4000, sodium citrate, Bis-Tris Propane, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | beta-catenin peptide | 5 (mg/ml) | |
3 | 1 | reservoir | PEG4000 | 16-20 (%) | |
4 | 1 | reservoir | sodium citrate | 320 (mM) | |
5 | 1 | reservoir | BTP | 100 (mM) | pH6.8 |