1O6P
Importin Beta bound to a GLFG Nucleoporin peptide
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 | 125.820, 67.030, 129.260 |
Unit cell angles | 90.00, 98.99, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.238 |
Rwork | 0.238 |
R-free | 0.26900 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qgr |
RMSD bond length | 0.013 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.400 | |
High resolution limit [Å] | 2.800 | 2.800 * |
Rmerge | 0.062 | 0.314 * |
Total number of observations | 257406 * | |
Number of reflections | 48209 | |
<I/σ(I)> | 7.9 | |
Completeness [%] | 91.8 | 89.6 * |
Redundancy | 2.6 | 2.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 100MM AMMONIUM ACETATE PH6.0, 1.2M AMMONIUM SULPHATE, pH 6.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | peptide | 25 (mM) | |
3 | 1 | reservoir | ammonium acetate | 100 (mM) | pH6.0 |
4 | 1 | reservoir | ammonium sulfate | 1.2 (M) |