Abstract
The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal α-helix has been solved to 1.67 Å resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the α-helix by formation of a previously uncharacterized bulge, which we term the α aneurism. A conformational search of known protein structures has identified the α aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins.
Original language | English (US) |
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Pages (from-to) | 3275-3279 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 90 |
Issue number | 8 |
DOIs | |
State | Published - Apr 15 1993 |
ASJC Scopus subject areas
- General