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2FMA

Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 14-BM-C
Synchrotron siteAPS
Beamline14-BM-C
Temperature [K]100
Detector technologyCCD
Collection date2004-07-20
DetectorADSC QUANTUM 4
Wavelength(s)0.9
Spacegroup nameP 21 21 21
Unit cell lengths31.289, 32.488, 50.088
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution13.850 - 0.850
R-factor0.1305
Rwork0.131
R-free0.14970
Structure solution methodRigid body refinement
Starting model (for MR)2fjz
RMSD bond length0.026
RMSD bond angle0.036
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHELX
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0000.870
High resolution limit [Å]0.8500.850
Number of reflections41418
<I/σ(I)>1.7
Completeness [%]90.543.8
Redundancy1.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP82950.1M HEPES pH 8.0, 28-32% (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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