Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength

@article{Turner1998StructureDO,
  title={Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength},
  author={Mary Alice Turner and C S Yuan and Ronald T. Borchardt and Michael Hershfield and G. David Smith and P. Lynne Howell},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={369-376}
}
S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolyzing the potent feedback inhibitor AdoHcy to homocysteine and adenosine. The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium… Expand
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