6X2W
Crystal Structure of PKINES peptide bound to CRM1(E571K)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2017-06-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 106.586, 106.586, 302.710 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.124 - 3.001 |
| R-factor | 0.2005 |
| Rwork | 0.197 |
| R-free | 0.25310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hb2 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.528 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.050 |
| High resolution limit [Å] | 3.000 | 8.130 | 3.000 |
| Rmerge | 0.210 | 0.049 | 1.208 |
| Rmeas | 0.225 | 0.053 | 1.332 |
| Rpim | 0.078 | 0.018 | 0.548 |
| Total number of observations | 252900 | ||
| Number of reflections | 33391 | 1767 | 1687 |
| <I/σ(I)> | 3.6 | ||
| Completeness [%] | 92.7 | 86.8 | 95 |
| Redundancy | 7.6 | 7.5 | 5.6 |
| CC(1/2) | 0.998 | 0.536 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 273 | 17% (weight/vol) PEG3350, 100 mM Bis-Tris (pH 6.4), 200 mM ammonium nitrate, and 10 mM Spermine HCl |
