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The structure of porcine β-lactoglobulin shows a novel and unusual dimerization motif not previously seen in members of the lipocalin family. This partially explains the markedly different physicochemical properties of porcine and bovine β-lactoglobulin, despite these proteins sharing 66% amino-acid identity.

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Progress in the development of nanocrystallography is discussed and the remaining bottlenecks are highlighted.
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