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Crystallization and preliminary X‐ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis
Author(s) -
Ju Hansol,
Pandian Ramesh,
Kim Kyungmin,
Kim Kyeong Kyu,
Kim T. Doohun
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14004142
Subject(s) - bacillus licheniformis , crystallization , hydrolase , escherichia coli , chemistry , tetragonal crystal system , enzyme , crystallography , chromatography , crystal structure , biochemistry , bacteria , biology , organic chemistry , bacillus subtilis , genetics , gene
With increasing demand in biotechnological applications, the identification and characterization of novel lipolytic enzymes are of great importance. The crystallization and preliminary X‐ray crystallographic study of a novel type of hydrolase from Bacillus licheniformis (BL28) are described here. Recombinant BL28 protein containing a C‐terminal His tag was overproduced in Escherichia coli and purified to homogeneity. BL28 was crystallized using 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 30%( w / v ) PEG 4000 as a crystallizing solution. X‐ray diffraction data were collected to a resolution of 1.67 Å with an R merge of 5.8%. The BL28 crystals belonged to the tetragonal space group P 4 1 2 1 2, with unit‐cell parameters a = b = 57.89, c = 167.25 Å. A molecular‐replacement solution was obtained and structure refinement of BL28 is in progress.