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1P3B

Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-07-06
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths106.180, 109.520, 182.441
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution35.000 - 3.000
Rwork0.219
R-free0.29000

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1aoi
RMSD bond length0.007
RMSD bond angle1.190
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]35.0003.070
High resolution limit [Å]3.0003.000
Rmerge0.0590.271
Number of reflections43674

*

<I/σ(I)>14.32.8
Completeness [%]99.9

*

99.8
Redundancy4.98
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

620

*

Luger, K., (1997) Nature, 389, 251.

*

Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111MnCl2
211KCl
311Potassium cacodylate
412MnCl2
512KCl
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein4 (mg/ml)
21drop50 (mM)
31drop70-75 (mM)
41droppotassium cacodylate20 (mM)pH6.0
51reservoir40-46 (mM)
61reservoir35-40 (mM)
71reservoirpotassium cacodylate20 (mM)pH6.0

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