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Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis.

ABSTRACT: 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 Rmerge of 5.8%. The BL28 crystals belonged to the tetragonal space group P41212, 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.

SUBMITTER: Ju H

PROVIDER: S-EPMC3976066 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis.

Ju Hansol H Pandian Ramesh R Kim Kyungmin K Kim Kyeong Kyu KK Kim T Doohun TD

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4

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 tribas ...[more]

PMID: 24699742

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