4RIL

Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 68-78, determined by electron diffraction

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ELECTRON MICROSCOPE
Source details	TECNAI F20 TEM
Temperature [K]	100
Detector technology	CMOS
Collection date	2014-08-28
Detector	TVIPS F416 CMOS CAMERA
Wavelength(s)	0.0251
Spacegroup name	C 1 2 1
Unit cell lengths	70.810, 4.820, 16.790
Unit cell angles	90.00, 105.68, 90.00

Refinement procedure

Resolution	16.430 - 1.430
R-factor	0.2512
Rwork	0.248
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4rik
RMSD bond length	0.010
RMSD bond angle	1.650
Data reduction software	XDS
Data scaling software	Aimless (0.3.11)
Phasing software	PHASER (2.5.6)
Refinement software	BUSTER-TNT (BUSTER 2.10.0)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	16.430	16.430	1.600
High resolution limit [Å]	1.430	3.200	1.430
Rmerge	0.175	0.080	0.565
Total number of observations		478	1245
Number of reflections	1073
<I/σ(I)>	5.5	13	2.5
Completeness [%]	89.9	94	82.5
Redundancy	4.4	3.8	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	batch crystallization	4	310	1 mg of synthetic peptide GAVVTGVTAVA was dissolved in 1 ml of sterile water and shaken overnight in an orbital mixing plate, pH 4.0, batch crystallization, temperature 310K