6XNM

GCN4-p1 Peptide Trimer with tyrosine residue at position 16

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-003
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-09-01
Detector	DECTRIS PILATUS 200K
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	59.553, 34.482, 46.936
Unit cell angles	90.00, 100.65, 90.00

Refinement procedure

Resolution	13.770 - 2.250
R-factor	0.2383
Rwork	0.225
R-free	0.35810
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1swi
RMSD bond length	0.009
RMSD bond angle	1.293
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX (1.16_3549)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	13.770	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.041	0.090
Rmeas	0.059	0.127
Rpim	0.041	0.090
Number of reflections	7950	818
<I/σ(I)>	20.01	9.6
Completeness [%]	91.5	91.42
Redundancy	1.9	1.9
CC(1/2)	0.996	0.942

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.