5UWJ
Crystal Structure of FMRP 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 | CCD |
Collection date | 2015-02-07 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9795 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 106.493, 106.493, 303.928 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.625 - 2.221 |
R-factor | 0.181 |
Rwork | 0.180 |
R-free | 0.21350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hb2 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.631 |
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 | 2.260 |
High resolution limit [Å] | 2.220 | 2.220 |
Rmerge | 0.077 | 0.966 |
Rpim | 0.033 | 0.408 |
Number of reflections | 86622 | 4266 |
<I/σ(I)> | 21.6 | 2.1 |
Completeness [%] | 99.4 | 100 |
Redundancy | 6.2 | |
CC(1/2) | 0.669 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 295 | 17% PEG3350, 100 mM Bis-Tris, pH 6.4, 200 mM ammonium nitrate, 10 mM spermine-HCl, 4 mM HCl |