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Title: Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach. Author: Martini VP, Glogauer A, Iulek J, Souza EM, Pedrosa FO, Krieger N. Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Feb 01; 68(Pt 2):175-7. PubMed ID: 22297992. 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.[Abstract] [Full Text] [Related] [New Search]