6V7M

Crystal structure of a proteolytically cleaved, amino terminal domain of apolipoprotein E3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1993-06-15
Detector	SDMS
Wavelength(s)	1.54
Spacegroup name	P 21 21 21
Unit cell lengths	41.330, 54.450, 86.670
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.000 - 2.000
R-factor	0.2054
Rwork	0.203
R-free	0.25980
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nfn
RMSD bond length	0.006
RMSD bond angle	1.287
Data reduction software	SDMS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0253)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.330	2.060
High resolution limit [Å]	2.000	2.010
Rmerge	0.241	0.528
Rmeas	0.277	0.747
Rpim	0.127	0.528
Number of reflections	11748	207
<I/σ(I)>	3.9	1.1
Completeness [%]	86.0
Redundancy	3.8
CC(1/2)	0.968	0.096

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.8	298	Crystallization was by sitting drop vapor diffusion in Cryschem plates at room temperature. Reservoirs were 16% to 18 % 2-methyl-2,4-pentanediol (MPD) buffered with 0.1 M sodium acetate at pH 5.8 and including 0.25% octyl-beta-D-1-thioglucopyranoside. The droplets were initial composed of equal amounts of the reservoir and an 8 mg/ml solution of the protein in 0.02 M ammonium carbonate.