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