5H2V
Crystal structure of the karyopherin Kap121p bound to the SUMO protease Ulp1p
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-12-04 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.830, 124.710, 130.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.713 - 2.800 |
| R-factor | 0.2001 |
| Rwork | 0.198 |
| R-free | 0.24120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3w3w |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.889 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless (0.1.27) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 36.710 | 36.710 | 2.950 |
| High resolution limit [Å] | 2.800 | 8.850 | 2.800 |
| Rmerge | 0.167 | 0.050 | 0.728 |
| Rmeas | 0.180 | ||
| Rpim | 0.067 | ||
| Total number of observations | 224445 | ||
| Number of reflections | 31520 | ||
| <I/σ(I)> | 8.4 | ||
| Completeness [%] | 100.0 | 98.7 | 100 |
| Redundancy | 7.1 | 6.4 | 7.2 |
| CC(1/2) | 0.995 | 0.997 | 0.778 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1M HEPES, 10% 2-propanol, 24% PEG20000 |
