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TitleCrystal Structures of a T4-lysozyme Duplication-extension Mutant Demonstrate that the Highly Conserved beta-Sheet Region has Low Intrinsic Folding Propensity
Journal, issue, pagesJ. Mol. Biol., Vol. 316, Page 931-940, Year 2002
Publish dateAug 21, 2001 (structure data deposition date)
AuthorsSagermann, M. / Matthews, B.W.
External linksJ. Mol. Biol. / PubMed:11884133
MethodsX-ray diffraction
Resolution1.9 - 2.3 Å
Structure data

PDB-1jtm:
Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet has Weak Intrinsic Folding Propensity
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1jtn:
Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE / SEQUENCE DUPLICATION / CONTEXT DEPENDENT FOLDING / SEQUENCE REPEAT

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