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Protein Science, Vol 1, Issue 8 1073-1077, Copyright © 1992 by Cold Spring Harbor Laboratory Press


ARTICLE

Crystallization of proton channel peptides

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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