6XNE

GCN4-p1 Peptide Trimer with p-methylphenylalanine residue at position 16 (me-F16)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-003
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-03-28
Detector	DECTRIS PILATUS 200K
Wavelength(s)	1.54
Spacegroup name	C 1 2 1
Unit cell lengths	60.138, 34.891, 47.041
Unit cell angles	90.00, 100.63, 90.00

Refinement procedure

Resolution	20.100 - 1.960
R-factor	0.2247
Rwork	0.210
R-free	0.30860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1swi
RMSD bond length	0.008
RMSD bond angle	0.893
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.100	2.037
High resolution limit [Å]	1.960	1.966
Rmerge	0.051	0.329
Rmeas	0.072	0.465
Rpim	0.051	0.329
Number of reflections	13582	1201
<I/σ(I)>	19.02	3.26
Completeness [%]	99.5	97.68
Redundancy	2	1.8
CC(1/2)	0.992	0.623

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 me-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0.