Title : Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis - Ju_2014_Acta.Crystallogr.F.Struct.Biol.Commun_70_473 |
Author(s) : Ju H , Pandian R , Kim K , Kim KK , Kim TD |
Ref : Acta Crystallographica F Struct Biol Commun , 70 :473 , 2014 |
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 A 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 A. A molecular-replacement solution was obtained and structure refinement of BL28 is in progress. |
PubMedSearch : Ju_2014_Acta.Crystallogr.F.Struct.Biol.Commun_70_473 |
PubMedID: 24699742 |
Gene_locus related to this paper: bacld-q65eq1 |
Gene_locus | bacld-q65eq1 |
Ju H, Pandian R, Kim K, Kim KK, Kim TD (2014)
Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis
Acta Crystallographica F Struct Biol Commun
70 :473
Ju H, Pandian R, Kim K, Kim KK, Kim TD (2014)
Acta Crystallographica F Struct Biol Commun
70 :473