Bian_2005_Biochim.Biophys.Acta_1752_99

Reference

Title : Purification and preliminary crystallographic analysis of a Penicillium expansum lipase - Bian_2005_Biochim.Biophys.Acta_1752_99
Author(s) : Bian C , Yuan C , Lin L , Lin J , Shi X , Ye X , Huang Z , Huang M
Ref : Biochimica & Biophysica Acta , 1752 :99 , 2005
Abstract :

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 method of vapor diffusion with ammonia sulfate as the precipitating agent at 298 K. The crystals have tetragonal lattice and unit-cell parameters of a=b=88.09 A, c=126.54 A. Diffraction data were collected to a resolution of 2.08 A on an in-house rotating-anode generator.

PubMedSearch : Bian_2005_Biochim.Biophys.Acta_1752_99
PubMedID: 16112629

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Citations formats

Bian C, Yuan C, Lin L, Lin J, Shi X, Ye X, Huang Z, Huang M (2005)
Purification and preliminary crystallographic analysis of a Penicillium expansum lipase
Biochimica & Biophysica Acta 1752 :99

Bian C, Yuan C, Lin L, Lin J, Shi X, Ye X, Huang Z, Huang M (2005)
Biochimica & Biophysica Acta 1752 :99