Journal:Acta Cryst D:S2059798320008116
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[[Image:Fig-4-CD-final-edit7.png|thumb|400px|left|(a) Circular dichroism spectra of freshly prepared and intact BibA34–400 sample at 20°C (red), at 40°C (orange) and denatured at 80°C followed by cooling to 20°C (green), the standard deviation error between the BibA34–400 samples (gray dotted line) and the spectrum generated from the BibA126–398 crystal structure (black). Two negative peaks at 208 and 222 nm typical of a α-helical secondary structure were observed for the BibA34–400 sample. (b) Estimated secondary-structure content (%) of BibA34–400 sample in solution (top) and the spectrum generated from the BibA126–398 crystal structure (bottom).]] | [[Image:Fig-4-CD-final-edit7.png|thumb|400px|left|(a) Circular dichroism spectra of freshly prepared and intact BibA34–400 sample at 20°C (red), at 40°C (orange) and denatured at 80°C followed by cooling to 20°C (green), the standard deviation error between the BibA34–400 samples (gray dotted line) and the spectrum generated from the BibA126–398 crystal structure (black). Two negative peaks at 208 and 222 nm typical of a α-helical secondary structure were observed for the BibA34–400 sample. (b) Estimated secondary-structure content (%) of BibA34–400 sample in solution (top) and the spectrum generated from the BibA126–398 crystal structure (bottom).]] | ||
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| + | [[Image:Fig5a-c-relabel-motifs-photoshop-edit.png|thumb|400px|left|(a) Pair distance distribution [P(r)] function of intact BibA34–400 protein. (b) Comparison of the experimental scattering profile (in blue) for BibA34–400 with profiles from a theoretical model (FoXS; green) derived from the proposed BibA34–400 model. (c) Fit of the crystal structure of BibA126–398 (cyan) and the proposed BibA34–400 (magenta) into the ab initio model of BibA34–400 calculated with ''DAMMIF''.]] | ||
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<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:29, 13 August 2020
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