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1OR2

APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]125
Detector technologyAREA DETECTOR
Collection date1997-04-15
DetectorADSC
Spacegroup nameP 21 21 21
Unit cell lengths47.680, 55.590, 63.590
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 2.500
R-factor0.252

*

Rwork0.267
R-free0.29700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1bz4
RMSD bond length0.016
RMSD bond angle2.500

*

Data reduction softwareUCSD-system (DATA REDUCTION PACKAGE)
Data scaling softwareUCSD-system
Phasing softwareEPMR
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.680
High resolution limit [Å]2.4902.490
Rmerge0.0690.245
Total number of observations39148

*

Number of reflections5913
<I/σ(I)>29.74.4
Completeness [%]93.889.5

*

Redundancy6.64
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.629350MM 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
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG40020-25 (%)
21reservoirsodium cacodylate50 (mM)
31drop20 (mM)
41dropprotein5 (mg/ml)

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