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5E61

Structure of amyloid-forming peptide FGAILSS (residues 23-29) from islet amyloid polypeptide

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 24-ID-E
Synchrotron siteAPS
Beamline24-ID-E
Temperature [K]291
Detector technologyCCD
Collection date2014-04-25
DetectorADSC QUANTUM 315
Wavelength(s)0.979
Spacegroup nameP 1
Unit cell lengths8.770, 9.500, 24.740
Unit cell angles88.22, 80.00, 70.34
Refinement procedure
Resolution4.380 - 1.790
R-factor0.17221
Rwork0.167
R-free0.21833
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.016
RMSD bond angle2.000
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwarePHASER
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]4.3801.960
High resolution limit [Å]1.7901.790
Rmerge0.2410.696
Number of reflections647
<I/σ(I)>4.291.4
Completeness [%]93.472.3
Redundancy5.217
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP2916.4mg/ml in 20mM Lithium hydroxide and mixed with 0.1M HEPES pH 6.5 and 0.5M Sodium Formate

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PDB entries from 2024-05-15

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