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Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (B. mori L.) haemolymph, have been determined. The haemolymph-isolated protein was identified through successful sequence assignment according to electron-density maps at 1.33 Å resolution.

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Four crystal structures of bovine, equine (two crystal forms) and leporine serum albumin have been determined at resolutions of 2.04-2.47 Å. The proteins were isolated from animal blood and additionally defatted and purified.
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