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Structure paper

TitleStabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.
Journal, issue, pagesPlos One, Vol. 6, Page e21624-e21624, Year 2011
Publish dateJan 18, 2010 (structure data deposition date)
AuthorsChan, C.H. / Yu, T.H. / Wong, K.B.
External linksPlos One / PubMed:21720566
MethodsX-ray diffraction
Resolution1.8 - 2 Å
Structure data

PDB-3lfo:
Crystal structure of T. celer L30e E90A/R92A variant
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3ra5:
Crystal structure of T. celer L30e E6A/R92A variant
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3ra6:
Crystal structure of T. celer L30e E62A/K46A variant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • thermococcus celer (archaea)
KeywordsRIBOSOMAL PROTEIN / L30e / Thermophilic / globular protein

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