Resumen
A 5.5-Å resolution crystal structure of an intensely sweet protein, monellin, has been determined on the basis of four isomorphous heavy-atom derivatives. The structure reveals many protruded features unlike most globular proteins. There are four monellin molecules in the asymmetric unit of the crystal and two dimer molecules related by a noncrystallographic twofold axis.
Idioma original | English (US) |
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Páginas (desde-hasta) | 5772-5774 |
Número de páginas | 3 |
Publicación | Biochemistry |
Volumen | 22 |
N.º | 25 |
DOI | |
Estado | Published - 1983 |
Publicado de forma externa | Sí |
ASJC Scopus subject areas
- Biochemistry