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


Citation

Mohd Shariff, Fairolniza and Raja Abdul Rahman, Raja Noor Zaliha and Mohamad Ali, Mohd Shukuri and Leow, Adam Thean Chor and Basri, Mahiran and Salleh, Abu Bakar (2010) Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (pt.6). pp. 715-717. ISSN 1744-3091

Abstract

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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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.1107/S174430911001482X
Publisher: International Union of Crystallography
Keywords: Lipases; L2 lipase; Bacillus sp. L2; Thermostable lipase; Counter-diffusion method
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 18 Jun 2015 00:15
Last Modified: 28 Sep 2016 02:41
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1107/S174430911001482X
URI: http://psasir.upm.edu.my/id/eprint/13836
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