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The structure of an acidic PLA2 from D. acutus been determined by molecular replacement with significant conformational differences observed in segment 14-23 of the two molecules in the asymmetric unit. This segment is related to the interface recognition site.

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SeMet S100A4 (human) has been crystallized using similar conditions to those used for the native protein. SeMet S100A4 crystals diffract better than the native for data collection and belong to space group P6 or P3.

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Crystallization of human S100P in high protein concentration was reported. Crystals diffract to 2.0 Å and belong to space group P41212.
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