Literature DB >> 11717508

Preliminary crystallographic studies of the double-stranded DNA-binding protein Sso10b from Sulfolobus solfataricus.

B N Wardleworth1, R J Russell, M F White, G L Taylor.   

Abstract

Crystals of Sso10b from the hyperthermophilic archaeon Sulfolobus solfataricus have been grown that diffract to 2.6 A resolution. The protein is a highly abundant non-specific double-stranded DNA-binding protein, conserved throughout the archaea, that has been implicated in playing a role in the architecture of archaeal chromatin.

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Year:  2001        PMID： 11717508     DOI： 10.1107/s0907444901015517

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN： 0907-4449


  4 in total

1.  Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms.

Authors:  Chia-Cheng Chou; Ting-Wan Lin; Chin-Yu Chen; Andrew H-J Wang
Journal:  J Bacteriol       Date:  2003-07       Impact factor: 3.490

2.  Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus.

Authors:  Michael M Brent; Ayaka Iwata; Juliana Carten; Kehao Zhao; Ronen Marmorstein
Journal:  J Biol Chem       Date:  2009-05-27       Impact factor: 5.157

3.  Dimer-dimer stacking interactions are important for nucleic acid binding by the archaeal chromatin protein Alba.

Authors:  Clare Jelinska; Biljana Petrovic-Stojanovska; W John Ingledew; Malcolm F White
Journal:  Biochem J       Date:  2010-03-15       Impact factor: 3.857

4.  Structure of Alba: an archaeal chromatin protein modulated by acetylation.

Authors:  B N Wardleworth; R J M Russell; S D Bell; G L Taylor; M F White
Journal:  EMBO J       Date:  2002-09-02       Impact factor: 11.598
  4 in total

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