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2FJZ

Structure of the Alzheimer's Amyloid Precursor Protein (APP) copper binding domain (residues 133 to 189) in 'small unit cell' form, metal-free

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]105
Detector technologyAREA DETECTOR
Collection date2003-02-20
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths31.346, 32.518, 50.200
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution22.570 - 1.610
R-factor0.177
Rwork0.177
R-free0.20900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1owt
RMSD bond length0.013
RMSD bond angle1.300
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.670
High resolution limit [Å]1.6101.610
Number of reflections7043
<I/σ(I)>15.55.4
Completeness [%]96.386.9
Redundancy2.72.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP829528 - 32 % (w/v) PEG 10000, 0.1 M HEPES pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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