Ontology highlight
ABSTRACT:
SUBMITTER: Makin OS
PROVIDER: S-EPMC544296 | biostudies-literature | 2005 Jan
REPOSITORIES: biostudies-literature
Makin O Sumner OS Atkins Edward E Sikorski Pawel P Johansson Jan J Serpell Louise C LC
Proceedings of the National Academy of Sciences of the United States of America 20050103 2
The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 A) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel beta-sheets in a cross-beta arrangement, chara ...[more]