1MWP

N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-06
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	31.200, 48.600, 67.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.800
Rwork	0.203
R-free	0.24200
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	26.920 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.032	0.178
Total number of observations	29942 *
Number of reflections	9710
<I/σ(I)>	28.3	7.4
Completeness [%]	95.0	98
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	22 *	pH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	5 (mM)
3	1	reservoir	PEG10000	22 (%)
4	1	reservoir	HEPES	100 (mM)