Open AccessCrystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach
Author(s) -
Martini V. P.,
Glogauer A.,
Iulek J.,
Souza E. M.,
Pedrosa F. O.,
Krieger N.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111051323
Subject(s) - crystallization , lipase , metagenomics , crystallography , materials science , computational biology , chemistry , biology , biochemistry , enzyme , gene , organic chemistry
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 P 4 1 22, with unit‐cell parameters a = b = 58.62, c = 192.60 Å.