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Structure paper

TitlePerturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties.
Journal, issue, pagesProteins, Vol. 15, Page 401-412, Year 1993
Publish dateJul 13, 1992 (structure data deposition date)
AuthorsPjura, P. / McIntosh, L.P. / Wozniak, J.A. / Matthews, B.W.
External linksProteins / PubMed:8460110
MethodsX-ray diffraction
Resolution1.8 - 1.95 Å
Structure data

PDB-1l00:
PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1l98:
PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1l99:
PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-HOH:
WATER

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

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