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Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution
A Mondragón1, S Subbiah, S C Almo
1Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.
Journal of Molecular Biology
|January 5, 1989
Abstract:
The crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.