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4RP6

Structure of the amyloid-forming segment LTIITLE from p53 (residues 252-258)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 24-ID-E
Synchrotron siteAPS
Beamline24-ID-E
Temperature [K]100
Detector technologyCCD
Collection date2012-02-12
DetectorADSC QUANTUM 315
Wavelength(s)0.9792
Spacegroup nameP 1
Unit cell lengths4.811, 12.599, 21.340
Unit cell angles86.59, 89.29, 79.15
Refinement procedure
Resolution21.302 - 1.703
R-factor0.1655
Rwork0.163
R-free0.19190
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.080
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwarePHENIX ((phenix.refine: 1.7.3_928))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]21.3021.780
High resolution limit [Å]1.7031.720
Rmerge0.0960.505
Number of reflections512
<I/σ(I)>10.611.6
Completeness [%]97.091.4
Redundancy3.12.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5291reservoir contained 0.1 M Tris buffer pH 8.5 and 20% ethanol, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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