Structural analysis of polymers of sickle cell hemoglobin. III. Fibers within fascicles.
We have examined the structure of hemoglobin S fibers, which are associated into large bundles, or fascicles. Electron micrographs of embedded and cross-sectioned fascicles provide an end-on view of the component fibers. The cross-sectional images are rotationally blurred as a result of the twist of the fiber within the finite thickness of the section. We have applied restoration techniques to recover a deblurred image of the fiber. The first step in this procedure involved correlation averaging images of cross-sections of individual fibers in order to improve the signal-to-noise ratio. The rotationally blurred image was then geometrically transformed to polar co-ordinates. In this space, the rotational blur is transformed into a linear blur. The linearly blurred image is the convolution of the unblurred image and a point spread function that can be closely approximated by a square pulse. Deconvolution in Fourier space, followed by remapping to Cartesian co-ordinates, produced a deblurred image of the original micrograph. The deblurred images indicate that the fiber is comprised of 14 strands of hemoglobin S. This result provides confirmation of the fiber structure determined using helical reconstruction techniques and indicates that the association of fibers into ordered arrays does not alter their molecular structure.
Carragher
B
B
Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.
Bluemke
D A
DA
Becker
M
M
McDade
W A
WA
Potel
M J
MJ
Josephs
R
R
D006451:Hemoglobin, Sickle; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D011108:Polymers
D006451:Hemoglobin, Sickle; D046911:Macromolecular Substances; D011108:Polymers