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ABSTRACT:
SUBMITTER: Martini VP
PROVIDER: S-EPMC3274396 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
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]