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Crystallization and preliminary X‐ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2

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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 Å resolution using an in‐house Bruker X8 PROTEUM single‐crystal diffractometer system. The crystal belonged to the primitive orthorhombic space group P212121, with unit‐cell parameters a = 87.44, b = 94.90, c = 126.46 Å. The asymmetric unit contained one single molecule of protein, with a Matthews coefficient (V M) of 2.85 Å3 Da−1 and a solvent content of 57%.
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Keywords: Bacillus sp. L2; L2 lipase; counter‐diffusion method; lipases; thermostable lipase

Document Type: Research Article

Publication date: June 1, 2010

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