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4RP7

Structure of the amyloid-forming segment TIITLE from p53 (residues 253-258)

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 nameC 1 2 1
Unit cell lengths43.018, 4.849, 19.774
Unit cell angles90.00, 92.12, 90.00
Refinement procedure
Resolution21.494 - 1.576
R-factor0.1666
Rwork0.164
R-free0.19250
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.009
RMSD bond angle1.861
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]21.4941.650
High resolution limit [Å]1.5761.590
Rmerge0.1140.320
Number of reflections636
<I/σ(I)>8.914.12
Completeness [%]96.587.7
Redundancy43
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6291reservoir contained 0.01 M zinc chloride, 0.1 M MES buffer pH 6, and 20% PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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