5H2W
Crystal structure of the karyopherin Kap60p bound to the SUMO protease Ulp1p (150-340)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-11-30 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 |
| Unit cell lengths | 52.610, 63.540, 80.910 |
| Unit cell angles | 106.09, 107.72, 90.50 |
Refinement procedure
| Resolution | 27.028 - 2.500 |
| R-factor | 0.2152 |
| Rwork | 0.213 |
| R-free | 0.24660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c1t |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.822 |
| 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] | 30.370 | 30.370 | 2.600 |
| High resolution limit [Å] | 2.500 | 9.010 | 2.500 |
| Rmerge | 0.050 | 0.025 | 0.163 |
| Rmeas | 0.070 | ||
| Rpim | 0.050 | ||
| Total number of observations | 47966 | ||
| Number of reflections | 29881 | ||
| <I/σ(I)> | 5.9 | ||
| Completeness [%] | 90.5 | 91.3 | 91 |
| Redundancy | 1.6 | 1.9 | 1.7 |
| CC(1/2) | 0.995 | 0.996 | 0.956 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.1M MES, 0.1M calcium acetate, 12% PEG8000 |
