Purification and preliminary crystallographic analysis of a Penicillium expansum lipase.
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.
Bian
Chuanbing
C
State Key Lab on Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, 155 Yang Qiao Xi Lu, Fuzhou 350002, China.
Yuan
Cai
C
Lin
Lin
L
Lin
Junhan
J
Shi
Xiaoli
X
Ye
Xiaoming
X
Huang
Zixiang
Z
Huang
Mingdong
M
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
D008049:Lipase