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Purification and preliminary crystallographic analysis of a Penicillium expansum lipase

✍ Scribed by ChuanBing Bian; Cai Yuan; Lin Lin; JunHan Lin; XiaoLi Shi; XiaoMing Ye; ZiXiang Huang; MingDong Huang

Book ID
104003453
Publisher
Elsevier Science
Year
2005
Tongue
English
Weight
244 KB
Volume
1752
Category
Article
ISSN
1570-9639

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✦ Synopsis

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.

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