Bn. Wardleworth et al., Preliminary crystallographic studies of the double-stranded DNA-binding protein Sso10b from Sulfolobus solfataricus, ACT CRYST D, 57, 2001, pp. 1893-1894
Crystals of Sso10b from the hyperthermophilic archaeon Sulfolobus solfatari
cus have been grown that diffract to 2.6 Angstrom resolution. The protein i
s a highly abundant non-specific double-stranded DNA-binding protein, conse
rved throughout the archaea, that has been implicated in playing a role in
the architecture of archaeal chromatin.