5X8N
Crystal structure of mouse importin-alpha1 bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-17A |
Synchrotron site | Photon Factory |
Beamline | BL-17A |
Temperature [K] | 95 |
Detector technology | PIXEL |
Collection date | 2017-02-12 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.270, 90.290, 98.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.765 - 2.150 |
R-factor | 0.1865 |
Rwork | 0.185 |
R-free | 0.20990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wum |
RMSD bond length | 0.003 |
RMSD bond angle | 0.656 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.5.31) |
Phasing software | MOLREP |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.770 | 30.770 | 2.220 |
High resolution limit [Å] | 2.150 | 8.860 | 2.150 |
Rmerge | 0.086 | 0.034 | 0.964 |
Rmeas | 0.095 | 0.038 | 1.060 |
Rpim | 0.039 | 0.017 | 0.436 |
Total number of observations | 227759 | ||
Number of reflections | 38548 | ||
<I/σ(I)> | 13.1 | ||
Completeness [%] | 100.0 | 98.1 | 100 |
Redundancy | 5.9 | 5 | 5.8 |
CC(1/2) | 0.998 | 0.999 | 0.680 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | MES, sodium citrate, DTT |