Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.

@article{Clausen1996CrystalSO,
  title={Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.},
  author={Tim Clausen and Robert Huber and Bernd Laber and H. D. Pohlenz and Albrecht Messerschmidt},
  journal={Journal of molecular biology},
  year={1996},
  volume={262 2},
  pages={202-24}
}
Cystathionine beta-lyase (CBL) is a member of the gamma-family of PLP-dependent enzymes, that cleaves C beta-S bonds of a broad variety of substrates. The crystal structure of CBL from E. coli has been solved using MIR phases in combination with density modification. The structure has been refined to an R-factor of 15.2% at 1.83 A resolution using synchroton radiation diffraction data. The asymmetric unit of the crystal cell (space group C222(1)) contains two monomers related by 2-fold symmetry… CONTINUE READING

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