3OQS
Crystal structure of importin-alpha bound to a CLIC4 NLS peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-03-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.95 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.594, 89.558, 100.083 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.050 - 2.000 |
R-factor | 0.199 |
Rwork | 0.197 |
R-free | 0.23690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ial |
RMSD bond length | 0.020 |
RMSD bond angle | 1.672 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.9) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 66.739 | 21.051 | 2.110 |
High resolution limit [Å] | 2.000 | 6.320 | 2.000 |
Rmerge | 0.041 | 0.776 | |
Rmeas | 0.045 | 0.871 | |
Rpim | 0.018 | 0.381 | |
Total number of observations | 10551 | 27080 | |
Number of reflections | 46758 | ||
<I/σ(I)> | 12.2 | 30.8 | 1.8 |
Completeness [%] | 96.7 | 97.2 | 80.3 |
Redundancy | 6.8 | 6.5 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | 0.7M sodium citrate, 10mM DTT, 70mM HEPES pH 7.4, vapor diffusion, hanging drop, temperature 293K |