These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • 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]