6X2X
Crystal Structure of Mek1NES 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 | 2017-08-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9795 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 106.749, 106.749, 303.824 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.207 - 2.458 |
R-factor | 0.2016 |
Rwork | 0.200 |
R-free | 0.25000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hb2 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.694 |
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 | 2.490 |
High resolution limit [Å] | 2.450 | 6.650 | 2.450 |
Rmerge | 0.096 | 0.042 | |
Rmeas | 0.098 | 0.042 | |
Rpim | 0.019 | 0.008 | 0.302 |
Total number of observations | 2248198 | ||
Number of reflections | 65125 | 3619 | 2796 |
<I/σ(I)> | 5.2 | ||
Completeness [%] | 99.3 | 99.8 | 86.4 |
Redundancy | 34.5 | 32.7 | 29.8 |
CC(1/2) | 0.998 | 0.727 |
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 |