Purification and preliminary crystallographic analysis of a Penicillium expansum lipase.

@article{Bian2005PurificationAP,
  title={Purification and preliminary crystallographic analysis of a Penicillium expansum lipase.},
  author={Chuanbing Bian and Cai Yuan and Lin Lin and Junhan Lin and Xiaoli Shi and Xiaoming Ye and Zixiang Huang and Mingdong Huang},
  journal={Biochimica et biophysica acta},
  year={2005},
  volume={1752 1},
  pages={99-102}
}
PF898 is a strain of Penicillium expansum optimized for the high level production of Penicillium expansum lipase (PEL). This PEL is unique compared with other lipases in several aspects, For example, the PEL shows low sequence identities (<30%) to all other known lipases, and high percentage of hydrophobic residues in the N-terminal region. The PEL was purified to homogeneity and shown to be 28 kDa by SDS-PAGE. Crystals suitable for X-ray diffraction analysis were obtained by the sitting-drop… CONTINUE READING