6X2P
Crystal Structure of the Mek1NES peptide bound to CRM1
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 | 2017-03-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | .9795 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 106.924, 106.924, 303.928 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.470 - 2.401 |
| R-factor | 0.2112 |
| Rwork | 0.210 |
| R-free | 0.25230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hb2 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.529 |
| 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 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
| Rmerge | 0.154 | 0.049 | |
| Rmeas | 0.157 | 0.050 | |
| Rpim | 0.050 | 0.010 | 0.584 |
| Total number of observations | 1815642 | ||
| Number of reflections | 69909 | 3867 | 3417 |
| <I/σ(I)> | 4.1 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 26 | 23.8 | 26.8 |
| CC(1/2) | 0.998 | 0.805 |
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 |
