Article
Solution structure and stability of the full-length excisionase from bacteriophage HK022.
European journal of biochemistry - 1 Dec 2003
Rogov Vladimir V, Lücke Christian, Muresanu Lucia, Wienk Hans, Kleinhaus Ioana, Werner Karla, Löhr Frank, Pristovsek Primoz, Rüterjans Heinz
Abstract excerpt
Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisionase protein (Xis) from the lambda-like bacteriophage HK022 and to study its sequence-specific DNA interaction. As wild-type Xis was previously characterized as a generally unstable protein, a biologically active HK022 Xis mutant with a single amino acid substitution Cys28-->Ser was used in this work....
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