1CQN

PROTEIN AGGREGATION AND ALZHEIMER'S DISEASE: CRYSTALLOGRAPHIC ANALYSIS OF THE PHENOMENON. ENGINEERED VERSION OF THE RIBOSOMAL PROTEIN S6 USED AS A STABLE SCAFFOLD TO STUDY OLIGOMERIZATION.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-02-27
Detector	MARRESEARCH
Spacegroup name	P 64 2 2
Unit cell lengths	82.821, 82.821, 141.583
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.218
Rwork	0.218
R-free	0.27600
RMSD bond length	0.005
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.076	0.296
Number of reflections	14676
<I/σ(I)>	11.1
Completeness [%]	84.0	83.2
Redundancy	1.8	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	8.5	293	PEG 400, SODIUM CITRATE, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 20K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	sodium citrate	0.2 (M)
2	1	1	Tris	0.1 (M)	pH8.5
3	1	1	PEG400	30 (%)
4	1	1	protein	6-8 (mg/ml)