4X1L

Structural basis for mutation-induced destabilization of Profilin 1 in ALS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-05
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	74.260, 31.840, 61.020
Unit cell angles	90.00, 122.66, 90.00

Refinement procedure

Resolution	27.895 - 2.160
R-factor	0.2173
Rwork	0.216
R-free	0.24690
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fik
RMSD bond length	0.002
RMSD bond angle	0.616
Data reduction software	XDS
Data scaling software	xia2
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.900	2.240
High resolution limit [Å]	2.160	2.160
Rmerge	0.075	0.589
Number of reflections	6584
<I/σ(I)>	13.3	2.3
Completeness [%]	99.3	98.9
Redundancy	3.2	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	PFN1 crystals were grown by hanging drop vapor diffusion after mixing the PFN1 protein with a 1:1 ratio of reservoir solution at 298K for WT. Reservoir solution for WT contained 50 mM KH2PO4, 36% (wt/vol) PEG 8,000 and 100 mM MES pH 6.0.