5DHA

Crystal Structure of CPEB4 NES Reverse Mutant 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	2015-02-20
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9795
Spacegroup name	P 43 21 2
Unit cell lengths	106.279, 106.279, 304.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.529 - 2.950
R-factor	0.1836
Rwork	0.181
R-free	0.24030
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	4hb2
RMSD bond length	0.003
RMSD bond angle	0.578
Data scaling software	HKL-2000
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	3.000
High resolution limit [Å]	2.950	8.000	2.950
Rmerge	0.115	0.038	0.893
Rmeas	0.125	0.041	0.986
Rpim	0.049	0.015	0.406
Total number of observations	222497
Number of reflections	36157
<I/σ(I)>	8.3
Completeness [%]	94.6	89.6	96
Redundancy	6.2	7.3	5.7
CC(1/2)		0.997	0.604

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	298	17% PEG3350, 100mM Bis-Tris, 10mM Spermine HCl