Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution
- 1 January 1987
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 193 (1) , 189-199
- https://doi.org/10.1016/0022-2836(87)90636-x
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolutionJournal of Molecular Evolution, 1985
- Thermodynamic stability and point mutations of bacteriophage T4 lysozymeJournal of Molecular Biology, 1984
- Intrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices and its relevance to membrane-bound proteinsJournal of Molecular Biology, 1984
- Structure and refinement of penicillopepsin at 1.8 Å resolutionJournal of Molecular Biology, 1983
- Molecular basis of thermostability in the lysozyme from bacteriophage T4Nature, 1979
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- Structure of the lysozyme from bacteriophage T4: An electron density map at 2.4 Å resolutionJournal of Molecular Biology, 1978
- Atomic coordinates for T4 phage lysozymeBiochemical and Biophysical Research Communications, 1977
- Exploring structural homology of proteinsJournal of Molecular Biology, 1976
- Crystallographic data for lysozyme from bacteriophage T4Journal of Molecular Biology, 1973