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1GS9

Apolipoprotein E4, 22k domain

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.2
Synchrotron siteALS
Beamline5.0.2
Temperature [K]125
Detector technologyCCD
Collection date1999-04-15
DetectorADSC CCD
Spacegroup nameP 21 21 21
Unit cell lengths45.511, 53.089, 73.372
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.900 - 1.700
R-factor0.219
Rwork0.218
R-free0.24700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1bz4
RMSD bond length0.016
RMSD bond angle1.794
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareEPMR
Refinement softwareREFMAC (5.0)
Data quality characteristics
 Overall
Low resolution limit [Å]20.900
High resolution limit [Å]1.700
Number of reflections20168
<I/σ(I)>12.1
Completeness [%]100.0
Redundancy7.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
15.650MM NA-CACODYLATE, PH 5.6, 20-25% PEG 400, 1% 2-ME, RT, CRYSTALLIZED FROM FULL LENGTH APOE4 CONSTRUCT (299 RESIDUES). PROTEOLYTIC CLEAVAGE IN CRYSTALLIZATION DROP TO 22K FRAGMENT. NEW, THIRD ORTHOGONAL CRYSTAL FORM OF APOE (ORTHO-3)

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