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The intriguing crystal organization of the domain-swapped dimer of a human pancreatic ribonuclease variant indicates that the protein can form fibrils in solution. They were observed and characterized by atomic force microscopy. The importance of domain swapping in inducing native-like fibril formation is highlighted.

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The structure of the thrombin-HD22-27mer complex, solved at 2.4 Å resolution, reveals an intriguing duplex-quadruplex folding of the aptamer, which extensively interacts with the exosite II of the protein.
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