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. 2012 Oct 8;7(10):e45847. doi: 10.1371/journal.pone.0045847

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© 2012 Felisberto-Rodrigues et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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. a) SAXS intensity as a function of the momentum transfer. This profile corresponds to the measurements taken at 4.7 mg/ml protein cocentration and pH 8.5. Average values are in red and the standard error in grey. b) The Kratky plot (see text for details) corresponds to a folded protein. c) Pair-distance distribution, P(r), function of the data shown in panel a). d) Three orthogonal views of the ab initio envelope calculated imposing orthorhombic symmetry.

Inline graphic — . a) SAXS intensity as a function of the momentum transfer. This profile corresponds to the measurements taken at 4.7 mg/ml protein cocentration and pH 8.5. Average values are in red and the standard error in grey. b) The Kratky plot (see text for details) corresponds to a folded protein. c) Pair-distance distribution, P(r), function of the data shown in panel a). d) Three orthogonal views of the ab initio envelope calculated imposing orthorhombic symmetry.