2OMM

GNNQQNY peptide corresponding to residues 7-13 of yeast prion sup35

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID13
Synchrotron site	ESRF
Beamline	ID13
Temperature [K]	100
Detector technology	CCD
Collection date	2005-07-16
Detector	MAR CCD 165 mm
Spacegroup name	P 21 21 21
Unit cell lengths	23.324, 4.934, 37.548
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.810 - 2.000
R-factor	0.242
Rwork	0.241
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1yjp
RMSD bond length	0.011
RMSD bond angle	1.544
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.810		2.200
High resolution limit [Å]	2.000	3.000	2.000
Rmerge	0.248	0.130	0.417
Number of reflections	380
<I/σ(I)>	4.61	8.1	2.7
Completeness [%]	96.4	97.1	98.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION, RECRYSTALLIZATION		298	peptide was dissolved at 10 mg/mL in water, quickly filtered, and left to sit at room temperature, EVAPORATION, RECRYSTALLIZATION, temperature 298K