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Protein Science, Vol 1, Issue 8 1073-1077, Copyright © 1992 by Cold Spring Harbor Laboratory Press
ARTICLE |
B. LOVEJOY, K. S. AKERFELDT, W. F. DEGRADO and D. EISENBERG
Molecular Biology Institute, University of California, Los Angeles, California 90024-1570
Crystals have been grown of two similar peptides that form ion-conducting channels in diphytanoyl phosphatidylcholine bilayers. These crystals were grown by slow evaporation of the organic solvent, 2,2,2-trifluoroethanol. Crystals of one of the peptides have been characterized by X-ray diffraction, and X-ray data have been measured to 2.3 A resolution. Earlier it was proposed that the ion-conducting channels formed by these peptides consist of four peptides associated as a parallel {alpha}-helical tetramer. On the basis of the space group and unit cell dimensions of the crystals, a packing scheme for the peptide is proposed that is consistent with a tetrameric channel.
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