2011
DOI: 10.1107/s1744309111002028
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Crystallization and preliminary X-ray crystallographic analysis of a thermostable organic solvent-tolerant lipase fromBacillussp. 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 Â 0.19 Â 0.08 mm.… Show more

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Cited by 2 publications
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“…Currently, only two thermostable lipases were reported grown by counter diffusion method, which are L42 lipase and L2 lipase. X-ray data of L42 lipase were collected at 2.0 Å and the crystal belonged to the monoclinic space group [ 15 ]. However thermostable L2 lipase crystal belonged to orthorhombic space group with resolution 2.7 Å [ 16 ].…”
Section: Resultsmentioning
confidence: 99%
“…Currently, only two thermostable lipases were reported grown by counter diffusion method, which are L42 lipase and L2 lipase. X-ray data of L42 lipase were collected at 2.0 Å and the crystal belonged to the monoclinic space group [ 15 ]. However thermostable L2 lipase crystal belonged to orthorhombic space group with resolution 2.7 Å [ 16 ].…”
Section: Resultsmentioning
confidence: 99%