1KYC

CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ELLIOTT GX-21
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-01-05
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	H 3 2
Unit cell lengths	33.386, 33.386, 65.691
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 1.450
Rwork	0.166
R-free	0.21700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hqj
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.500
High resolution limit [Å]	1.450	1.450
Rmerge	0.540 *
Total number of observations	47109 *
Number of reflections	2574
<I/σ(I)>	20	7
Completeness [%]	96.9 *	72.1
Redundancy	10	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	ammonium sulfate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	0.600 (mlsat)
2	1	reservoir	water	0.300 (ml)
3	1	reservoir	HEPES	1 (M)	pH7.5
4	1	drop	protein	60.0 (mg/ml)