6XNL

GCN4-p1 Peptide Trimer with iodo-phenylalanine residue at position 16 (IPF-F16)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2018-01-09
Detector	RDI CMOS_8M
Wavelength(s)	0.83
Spacegroup name	C 1 2 1
Unit cell lengths	59.069, 34.848, 46.712
Unit cell angles	90.00, 100.44, 90.00

Refinement procedure

Resolution	19.850 - 2.200
R-factor	0.2322
Rwork	0.222
R-free	0.32110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1swi
RMSD bond length	0.008
RMSD bond angle	1.146
Data reduction software	HKL-2000
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.16_3549)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.850	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.071	0.429
Rmeas	0.100	0.607
Rpim	0.071	0.429
Number of reflections	8716	695
<I/σ(I)>	14.32	2.67
Completeness [%]	97.9
Redundancy	1.8
CC(1/2)	0.986	0.462

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with IPF-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.