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Structure paper

TitleExploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment.
Journal, issue, pagesProtein Sci., Vol. 16, Page 842-851, Year 2007
Publish dateDec 5, 2006 (structure data deposition date)
AuthorsCellitti, J. / Llinas, M. / Echols, N. / Shank, E.A. / Gillespie, B. / Kwon, E. / Crowder, S.M. / Dahlquist, F.W. / Alber, T. / Marqusee, S.
External linksProtein Sci. / PubMed:17400926
MethodsX-ray diffraction
Resolution0.84 - 1.9 Å
Structure data

PDB-2o4w:
T4 lysozyme circular permutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2o79:
T4 lysozyme with C-terminal extension
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2o7a:
T4 lysozyme C-terminal fragment
Method: X-RAY DIFFRACTION / Resolution: 0.84 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-ACT:
ACETATE ION

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE / Protein folding / protein stability / protein engineering / T4 lysozyme / LYSOZYME / CIRCULAR PERMUTANT

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