title: Structure of phage 434 Cro protein at 2.35 A resolution.
abstract: The crystal structure of phage 434 Cro protein has been determined and refined against 2.35 A data to an R-factor of 19.5%. The protein comprises five alpha-helices and shows the helix-turn-helix motif found in other repressor proteins.
authors.affiliation: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.
authors.forename: A
authors.initials: A
authors.lastname: Mondragón
authors.forename: C
authors.initials: C
authors.lastname: Wolberger
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D001435:Bacteriophages / Q000235:genetics*; D004268:DNA-Binding Proteins; D004926:Escherichia coli; D008958:Models, Molecular; D008961:Models, Structural; D011487:Protein Conformation; D012097:Repressor Proteins / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics*; D054334:Viral Regulatory and Accessory Proteins; D014961:X-Ray Diffraction
chemical_list: D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins