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1I4M

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date1999-09-24
DetectorCUSTOM-MADE
Wavelength(s)1.0688
Spacegroup nameC 2 2 21
Unit cell lengths85.441, 85.707, 40.501
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 2.000
R-factor0.206
Rwork0.206
R-free0.25300
Structure solution methodMIR
RMSD bond length0.008

*

RMSD bond angle1.170

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMLPHARE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.070
High resolution limit [Å]2.0002.000
Rmerge0.0480.239
Number of reflections10069
<I/σ(I)>36
Completeness [%]96.784.8
Redundancy7.86
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

820

*

SODIUM CHLORIDE, TRIS HYDROCHLORIDE, CADMIUM CHLORIDE, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21reservoirTris-HCl0.1 (M)pH8.
31reservoir3 (M)
41reservoir5 (mM)

219869

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