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Crystallization and preliminary X-ray crystallographic analysis of a thermostable organic solvent-tolerant lipase from Bacillus sp. strain 42.

ABSTRACT: An organic solvent-tolerant lipase from Bacillus sp. strain 42 was crystallized using the capillary-tube method. The purpose of studying this enzyme was in order to better understand its folding and to characterize its properties in organic solvents. By initially solving its structure in the native state, further studies on protein-solvent interactions could be performed. X-ray data were collected at 2.0?Å resolution using an in-house diffractometer. The estimated crystal dimensions were 0.09×0.19×0.08?mm. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=117.41, b=80.85, c=99.44?Å, ?=96.40°.

SUBMITTER: Khusaini MS

PROVIDER: S-EPMC3053172 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of a thermostable organic solvent-tolerant lipase from Bacillus sp. strain 42.

Khusaini Mohd Saif MS Rahman Raja Noor Zaliha Raja Abd RN Mohamad Ali Mohd Shukuri MS Leow Thean Chor TC Basri Mahiran M Salleh Abu Bakar AB

Acta crystallographica. Section F, Structural biology and crystallization communications 20110225 Pt 3

An organic solvent-tolerant lipase from Bacillus sp. strain 42 was crystallized using the capillary-tube method. The purpose of studying this enzyme was in order to better understand its folding and to characterize its properties in organic solvents. By initially solving its structure in the native state, further studies on protein-solvent interactions could be performed. X-ray data were collected at 2.0 Å resolution using an in-house diffractometer. The estimated crystal dimensions were 0.09×0. ...[more]

PMID: 21393852

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