5H2X
Crystal structure of the karyopherin Kap60p bound to the SUMO protease Ulp1p (150-172)
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] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-06-14 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.570, 77.480, 114.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.268 - 2.200 |
| R-factor | 0.203 |
| Rwork | 0.202 |
| R-free | 0.22840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5h2w |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.738 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 49.270 | 49.270 | 2.270 |
| High resolution limit [Å] | 2.200 | 9.070 | 2.200 |
| Rmerge | 0.146 | 0.038 | 0.787 |
| Rmeas | 0.160 | ||
| Rpim | 0.065 | ||
| Total number of observations | 149220 | ||
| Number of reflections | 25386 | ||
| <I/σ(I)> | 9.9 | ||
| Completeness [%] | 100.0 | 99.6 | 100 |
| Redundancy | 5.9 | 4.8 | 6.1 |
| CC(1/2) | 0.995 | 0.998 | 0.777 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M sodium phosphate, 12% PEG8000 |
