Paper Report for: Martini_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_68_175
Reference
Title: Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach Martini VP, Glogauer A, Iulek J, Souza EM, Pedrosa FO, Krieger N Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 68:175, 2012 : PubMed
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 A resolution. The crystals belonged to the tetragonal space group P4(1)22, with unit-cell parameters a = b = 58.62, c = 192.60 A.
Martini VP, Glogauer A, Iulek J, Souza EM, Pedrosa FO, Krieger N (2012) Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach Acta Crystallographica Sect F Struct Biol Cryst Commun68: 175-7
Martini VP, Glogauer A, Iulek J, Souza EM, Pedrosa FO, Krieger N (2012) Acta Crystallographica Sect F Struct Biol Cryst Commun68: 175-7