2001Acta Crystallographica Section D Biological CrystallographyRequires access

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

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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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What this paper is about

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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Available 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.

Key concepts: Sulfolobus solfataricus, Sulfolobus, Archaea, DNA, Biology, Chromatin, DNA-binding protein, Biochemistry

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