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1P3L

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 lengths105.951, 109.612, 181.397
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 2.400
Rwork0.235
R-free0.26000

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1aoi
RMSD bond length0.011
RMSD bond angle1.460
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.460
High resolution limit [Å]2.4002.400
Rmerge0.0660.273
Number of reflections83303

*

<I/σ(I)>11.82.65
Completeness [%]98.7

*

96.8

*

Redundancy3.7
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

237992

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