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J Biol Chem, Vol. 273, Issue 29, 18429-18434, July 17, 1998
From the The three-dimensional structure of the cardiac
muscle ryanodine receptor (RyR2) is described and compared with its
skeletal muscle isoform (RyR1). Previously, structural studies of RyR2 have not been as informative as those for RyR1 because optimal conditions for electron microscopy, which require low levels of phospholipid, are destabilizing for RyR2. A simple procedure was devised for diluting RyR2 (in phospholipid-containing buffer) into a
lipid-free buffer directly on the electron microscope grid, followed by
freezing within a few seconds. Cryoelectron microscopy of RyR2 so
prepared yielded images of sufficient quality for analysis by single
particle image processing. Averaged projection images for RyR2, as well
as for RyR1, prepared under the same conditions, were found to be
nearly identical in overall dimensions and appearance at the resolution
attained,
Cryoelectron Microscopy and Image Analysis of the Cardiac
Ryanodine Receptor
,,,
,, and**
Wadsworth Center for Laboratories and
Research, New York State Department of Health, Albany, New York
12201-0509, the ** Department of Biomedical Sciences, School of Public
Health, State University of New York, Albany, New York 12222, and
the Department of Molecular Biology, Vanderbilt University,
Nashville, Tennessee 37235
30 Å. An initial three-dimensional reconstruction of RyR2
was determined (resolution 41 Å) and compared with previously
reported reconstructions of RyR1. Although they looked similar, which
is consistent with the similarity found for the projection images, and
with expectations based on the 66% amino acid sequence identity of the
two isoforms, structural differences near the corners of the
cytoplasmic assembly were observed in both two- and three-dimensional
studies.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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