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Structure paper

TitleEnhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Journal, issue, pagesNature, Vol. 336, Page 651-656, Year 1988
Publish dateMay 1, 1989 (structure data deposition date)
AuthorsNicholson, H. / Becktel, W.J. / Matthews, B.W.
External linksNature / PubMed:3200317
MethodsX-ray diffraction
Resolution1.7 - 1.85 Å
Structure data

PDB-1l19:
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1l20:
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

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

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