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