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 |