Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach.
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.
Department of Chemistry, Federal University of Paraná, Curitiba-PR, Brazil.
V P
VP
Martini
A
A
Glogauer
J
J
Iulek
E M
EM
Souza
F O
FO
Pedrosa
N
N
Krieger
D003460:Crystallization; D018360:Crystallography, X-Ray; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification; D056186:Metagenomics; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D008049:Lipase