5EKF
Crystallization and X-ray Diffraction Data Collection of Importin-alpha from Mus musculus Complexed with a XPG NLS Peptide, fragment 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-04-25 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.589, 89.542, 99.801 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.295 - 2.000 |
R-factor | 0.172 |
Rwork | 0.171 |
R-free | 0.19180 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.075 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (1.9_1692) |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 40.000 |
High resolution limit [Å] | 1.964 |
Number of reflections | 50196 |
<I/σ(I)> | 10.3 |
Completeness [%] | 99.4 |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.6-0.7 M sodium citrate, 10 mM DTT |