X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.

@article{Bewley1999XrayCA,
  title={X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.},
  author={Maria C. Bewley and Beatrice M. Tam and Jeffrey Grewal and Shouming He and Steven C Shewry and Michael E P Murphy and Anne B Mason and Robert Woodworth and Edward N Baker and R. T. MacGillivray},
  journal={Biochemistry},
  year={1999},
  volume={38 8},
  pages={2535-41}
}
The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris. The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution. This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian… CONTINUE READING