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1H0X

Structure of Alba: an archaeal chromatin protein modulated by acetylation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyAREA DETECTOR
Collection date2001-01-15
DetectorMSC
Spacegroup nameP 65 2 2
Unit cell lengths84.310, 84.310, 162.220
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.600
R-factor0.235
Rwork0.235
R-free0.28500
Structure solution methodMAD
RMSD bond length0.007
RMSD bond angle1.300
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.690
High resolution limit [Å]2.6002.600
Rmerge0.0460.320
Number of reflections10996
<I/σ(I)>6.92.7
Completeness [%]98.094.7

*

Redundancy7.67.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

6.5Wardleworth, B.N., (2001) Acta Crystallogr.,Sect.D, 57, 1893.

*

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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PDB entries from 2024-05-15

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