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Structure paper

TitleBiophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention.
Journal, issue, pagesProtein Sci., Vol. 21, Page 487-497, Year 2012
Publish dateMar 7, 2011 (structure data deposition date)
AuthorsAugustyniak, W. / Brzezinska, A.A. / Pijning, T. / Wienk, H. / Boelens, R. / Dijkstra, B.W. / Reetz, M.T.
External linksProtein Sci. / PubMed:22267088
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-3qzu:
Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • bacillus subtilis subsp. subtilis (bacteria)
KeywordsHYDROLASE / Alpha/beta hydrolase

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