Abstract
The three-dimensional structure of the lysozyme from bacteriophage T4 has been determined from a 2.4 Å resolution electron density map. The map, determined using isomorphous replacement and anomalous scattering differences from platinum and mercury-substituted crystals, reveals the approximate conformation of the molecule unambiguously. Details of the structure determination are presented and the conformation of the molecule is described in detail. The observed properties of those mutant lysozymes for which the changes in the amino acid sequence have been determined are discussed in the light of the three-dimensional structure. In most cases the behavior of the mutant lysozymes can be easily rationalized, but there are a few instances where this is not so.
Original language | English (US) |
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Pages (from-to) | 81-98 |
Number of pages | 18 |
Journal | Journal of Molecular Biology |
Volume | 118 |
Issue number | 1 |
DOIs | |
State | Published - Jan 5 1978 |
Funding
Mutant strains eJR14eJD5 and c,J28eJD8 wcrc kintlly provicktl by Drs A. Ts\lpt’itt ant1 M. B&la, rind cseHU58 by Dr D.-H. Liebscher. Tllis study was supported in part by grants from the National Institutes of Health (GM21967, GM19795, GM20066), the National Scienw Foundation (PCM75-18407), and a Public Health Service Career Development AwarcI to one of us (B.W.M.) (GM 70585) from tjlw Institutes of General Medical Sciancc-.
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology