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Structure paper

TitleElectrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values
Journal, issue, pagesPlos One, Vol. 7, Page e30296-e30296, Year 2012
Publish dateMay 24, 2010 (structure data deposition date)
AuthorsChan, C.H. / Wilbanks, C.C. / Makhatadze, G.I. / Wong, K.B.
External linksPlos One / PubMed:22279578
MethodsX-ray diffraction
Resolution2.3973 - 2.4 Å
Structure data

PDB-3n4y:
Crystal structure of wild-type T. celer L30e in low ionic strength condition without precipitant
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3n4z:
Crystal structure of quintuple Arg-to-Lys variant of T. celer L30e
Method: X-RAY DIFFRACTION / Resolution: 2.3973 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • thermococcus celer (archaea)
KeywordsRIBOSOMAL PROTEIN / L30e / thermophilic / low ionic strength / quintuple / Arg-to-Lys

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