1OR2

APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	125
Detector technology	AREA DETECTOR
Collection date	1997-04-15
Detector	ADSC
Spacegroup name	P 21 21 21
Unit cell lengths	47.680, 55.590, 63.590
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.500
R-factor	0.252 *
Rwork	0.267
R-free	0.29700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bz4
RMSD bond length	0.016
RMSD bond angle	2.500 *
Data reduction software	UCSD-system (DATA REDUCTION PACKAGE)
Data scaling software	UCSD-system
Phasing software	EPMR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.680
High resolution limit [Å]	2.490	2.490
Rmerge	0.069	0.245
Total number of observations	39148 *
Number of reflections	5913
<I/σ(I)>	29.7	4.4
Completeness [%]	93.8	89.5 *
Redundancy	6.6	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	50MM NA-CACODYLATE, PH 5.6, 10-20% PEG 400 AT ROOM TEMPERATURE. NO 2-ME ADDED. NOTE: WITH 2-ME OR LOWER PEG CONCENTRATIONS, OTHER CRYSTAL FORMS APPEARS (SEE PDB ENTRIES 1BZ4, 1OR3), VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	20-25 (%)
2	1	reservoir	sodium cacodylate	50 (mM)
3	1	drop		20 (mM)
4	1	drop	protein	5 (mg/ml)