Preliminary crystallographic studies of the double-stranded DNA-binding protein Sso10b fromSulfolobus solfataricus
Ben N. Wardleworth, Rupert J. Russell, Malcolm F. White, G.L. Taylor
Abstract
Ben N. Wardleworth, Rupert J. Russell, Malcolm 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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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.
Key concepts: Sulfolobus solfataricus, Sulfolobus, Archaea, DNA, Biology, Chromatin, DNA-binding protein, Biochemistry