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1H0Y

Structure of Alba: an archaeal chromatin protein modulated by acetylation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date2001-06-15
DetectorADSC CCD
Spacegroup nameI 41 2 2
Unit cell lengths84.680, 84.680, 87.140
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.800
R-factor0.251
Rwork0.251
R-free0.29500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1h0x
RMSD bond length0.009
RMSD bond angle1.300
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.900
High resolution limit [Å]2.8002.800
Rmerge0.0680.447

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Number of reflections4115
<I/σ(I)>15.62.4
Completeness [%]100.099.3

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Redundancy23.3

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23
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

5.6Wardleworth, B.N., (2001) Acta Crystallogr.,Sect.D, 57, 1893.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21dropTris50 (mM)pH7.5
31drop300 (mM)
41reservoirPEG800018 (%)
51reservoirsodium cacodylate0.1 (M)pH6.5
61reservoir0.2 (M)
71reservoir1,2,3-heptanetriol0.1 (M)

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