title: Preliminary crystallographic studies of the double-stranded DNA-binding protein Sso10b from Sulfolobus solfataricus.
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.
authors.affiliation: Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, Scotland.
authors.forename: B N
authors.initials: BN
authors.lastname: Wardleworth
authors.forename: R J
authors.initials: RJ
authors.lastname: Russell
authors.forename: M F
authors.initials: MF
authors.lastname: White
authors.forename: G L
authors.initials: GL
authors.lastname: Taylor
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D011487:Protein Conformation; D016944:Sulfolobus / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; C444360:Sso10b protein, Sulfolobus solfataricus