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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):401-3. doi: 10.1107/S1744309111002028. Epub 2011 Feb 25.

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, β=96.40°.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Bacterial Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Lipase / chemistry*
  • Molecular Sequence Data
  • Solvents / chemistry*
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Solvents
  • Lipase
  • thermostable lipase