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Structure paper

TitleEnhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 84, Page 6663-6667, Year 1987
Publish dateMay 1, 1989 (structure data deposition date)
AuthorsMatthews, B.W. / Nicholson, H. / Becktel, W.J.
External linksProc. Natl. Acad. Sci. USA / PubMed:3477797
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-1l23:
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1l24:
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE (O-GLYCOSYL)

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