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Structure paper

TitleStructural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1844, Page 632-640, Year 2014
Publish dateJun 4, 2013 (structure data deposition date)
AuthorsMerlino, A. / Russo Krauss, I. / Castellano, I. / Ruocco, M.R. / Capasso, A. / De Vendittis, E. / Rossi, B. / Sica, F.
External linksBiochim. Biophys. Acta / PubMed:24440460
MethodsX-ray diffraction
Resolution1.66 - 2.07 Å
Structure data

PDB-4l2a:
X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form II)
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

PDB-4l2b:
X-ray structure of the C57S mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-4l2c:
X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-4l2d:
X-ray structure of the Fe(II) form of the iron superoxide dismutase from Pseudoalteromonas haloplanktis
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FE2:
Unknown entry

Source
  • pseudoalteromonas haloplanktis (bacteria)
KeywordsOXIDOREDUCTASE / Superoxide dismutase / C57R mutant / C57S mutant

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