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Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach.


ABSTRACT: LipC12, a true lipase from family I.1 of bacterial lipases which was previously isolated through a metagenomics approach, contains 293 amino acids. Among lipases of known three-dimensional structure, it has a sequence identity of 47% to the lipase from Pseudomonas aeruginosa PAO1. Recombinant N-terminally His(6)-tagged LipC12 protein was expressed in Escherichia coli, purified in a homogenous form and crystallized in several conditions, with the best crystals being obtained using 2.0 M sodium formate and 0.1 M bis-tris propane pH 7.0. X-ray diffraction data were collected to 2.70 Å resolution. The crystals belonged to the tetragonal space group P4(1)22, with unit-cell parameters a = b = 58.62, c = 192.60 Å.

SUBMITTER: Martini VP 

PROVIDER: S-EPMC3274396 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach.

Martini V P VP   Glogauer A A   Iulek J J   Souza E M EM   Pedrosa F O FO   Krieger N N  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120126 Pt 2


LipC12, a true lipase from family I.1 of bacterial lipases which was previously isolated through a metagenomics approach, contains 293 amino acids. Among lipases of known three-dimensional structure, it has a sequence identity of 47% to the lipase from Pseudomonas aeruginosa PAO1. Recombinant N-terminally His(6)-tagged LipC12 protein was expressed in Escherichia coli, purified in a homogenous form and crystallized in several conditions, with the best crystals being obtained using 2.0 M sodium fo  ...[more]

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