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1P3A

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

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.2
Synchrotron siteALS
Beamline5.0.2
Temperature [K]100
Detector technologyCCD
Collection date2001-11-14
DetectorADSC QUANTUM 4
Wavelength(s)1.100
Spacegroup nameP 21 21 21
Unit cell lengths105.423, 109.721, 180.902
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 3.000
Rwork0.203
R-free0.26000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1aoi
RMSD bond length0.013
RMSD bond angle1.410
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0003.070
High resolution limit [Å]3.0003.000
Rmerge0.1000.282
Number of reflections42653

*

<I/σ(I)>16.17.6
Completeness [%]83.8

*

87.4

*

Redundancy4.3
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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PDB entries from 2024-05-15

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