2008
DOI: 10.1016/j.jmb.2008.02.020
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Structure of the Cytoskeleton of Spiroplasma melliferum BC3 and Its Interactions with the Cell Membrane

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Cited by 50 publications
(95 citation statements)
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“…This value is in very good agreement with the radius (∼50 Å) obtained from molecular mass by sequencing, 32 average protein density, linear mass density by STEM, 24 and diffractometry of single fibrils 13 and ribbons. 24,25 Thus, we establish a dimensional range in which structural or elliptical deviations from a near-circular base state (b/a ∼ 1) are allowed to a fairly large extent (b/a ∼ 1.05-1.6). Diffractograms of the images of bulk specimens yield an average of at least hundreds of tetramers per image field.…”
Section: Resultsmentioning
confidence: 98%
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“…This value is in very good agreement with the radius (∼50 Å) obtained from molecular mass by sequencing, 32 average protein density, linear mass density by STEM, 24 and diffractometry of single fibrils 13 and ribbons. 24,25 Thus, we establish a dimensional range in which structural or elliptical deviations from a near-circular base state (b/a ∼ 1) are allowed to a fairly large extent (b/a ∼ 1.05-1.6). Diffractograms of the images of bulk specimens yield an average of at least hundreds of tetramers per image field.…”
Section: Resultsmentioning
confidence: 98%
“…1b). Note that numerous images and diffractograms 13,22,24,25 of partially aligned ribbon bundles (equivalent to 'fiber diffraction') and random pellets of ribbons (equivalent to 'powder diffraction'), as well as those of single monolayered ribbons and individual fibrils, reveal the averages of axial and lateral spacings and their range of variability. The origins of the reflections in the diffractogram are the basic elliptical geometry (Fig.…”
Section: Resultsmentioning
confidence: 99%
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