Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis.

@article{Miller1996IdentificationOT,
  title={Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis.},
  author={Mitchell D Miller and Kurt L Krause},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 1},
  pages={24-33}
}
The Serratia endonuclease is an extracellularly secreted enzyme capable of cleaving both single- and double-stranded forms of DNA and RNA. It is the first member of a large class of related and usually dimeric endonucleases for which a structure is known. Using X-ray crystallography, the structure of monomer of this enzyme was reported by us previously (Miller MD et al., 1994, Nature Struct Biol 1:461-468). We now confirm the dimeric nature of this enzyme through light-scattering experiments… CONTINUE READING

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