5UWO
Crystal Structure of Engineered FMRP-1b NES Peptide in complex with CRM1-Ran-RanBP1
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 | PIXEL |
Collection date | 2016-02-19 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 106.475, 106.475, 304.314 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.071 - 2.347 |
R-factor | 0.1886 |
Rwork | 0.188 |
R-free | 0.22330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hb2 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.597 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.390 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.109 | |
Rpim | 0.039 | 0.571 |
Number of reflections | 74260 | 3658 |
<I/σ(I)> | 19 | 1.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.6 | 7.7 |
CC(1/2) | 0.444 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 295 | 16% PEG3350, 100 mM Bis-Tris, pH 6.4, 200 mM ammonium nitrate, 12 mM HCl |