Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2.
Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-diffusion method using 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl as precipitant. X-ray diffraction data were collected to 2.7 A resolution using an in-house Bruker X8 PROTEUM single-crystal diffractometer system. The crystal belonged to the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 87.44, b = 94.90, c = 126.46 A. The asymmetric unit contained one single molecule of protein, with a Matthews coefficient (V(M)) of 2.85 A(3) Da(-1) and a solvent content of 57%.
Shariff
Fairolniza Mohd
FM
Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Rahman
Raja Noor Zaliha Raja Abd
RN
Ali
Mohd Shukuri Mohamad
MS
Chor
Adam Leow Thean
AL
Basri
Mahiran
M
Salleh
Abu Bakar
AB
D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D008049:Lipase / Q000737:chemistry*
D001426:Bacterial Proteins; D008049:Lipase; C428386:thermostable lipase