Atomic structure of the Serratia marcescens endonuclease at 1.1 A resolution and the enzyme reaction mechanism.

@article{Shlyapnikov2000AtomicSO,
  title={Atomic structure of the Serratia marcescens endonuclease at 1.1 A resolution and the enzyme reaction mechanism.},
  author={S. V. Shlyapnikov and Vladimir V. Lunin and Markus Perbandt and Konstantin M Polyakov and Vladimir Y. Lunin and Vladimir M. Levdikov and Christian Betzel and Al'bert M Mikhailov},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2000},
  volume={56 Pt 5},
  pages={567-72}
}
The three-dimensional crystal structure of Serratia marcescens endonuclease has been refined at 1.1 A resolution to an R factor of 12.9% and an R(free) of 15.6% with the use of anisotropic temperature factors. The model contains 3694 non-H atoms, 715 water molecules, four sulfate ions and two Mg(2+)-binding sites at the active sites of the homodimeric protein. It is shown that the magnesium ion linked to the active-site Asn119 of each monomer is surrounded by five water molecules and shows an… CONTINUE READING

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