Solution structure of Archaeon DNA-binding protein ssh10b
A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b.
MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLADKIEIKEIRVGSQVVTSQ DGRQSRVSTIEIAIRKK
The chemical shift assignments of Ssh10b P62A mutant
The chemical shift assignments of Ssh10b protein
The structure was determined using triple-resonance NMR spectroscopy.
1.5mM Ssh10b U-95% 13C, U-98% 15N; 20mM acetate buffer;20mM KCl; 90%H2O,10% D2O
DNA BINDING, ARCHAEA, DNA BINDING PROTEIN
SSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQD GRQSRVSTIEIAIRKK