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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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The structures of GAPDH complexed with coenzyme analogues ADP-ribose and SNAD+ have been determined by molecular replacement. SNAD+-GAPDH reveals significant molecular asymmetry in the crystalline state.

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A non-toxic acidic phospholipase A2 from the venom of O. hannah (king cobra) has been crystallized and X-ray data have been collected and reduced to 2.1 Å resolution. Analysis by molecular replacement showed there to be six enzyme molecules per asymmetric unit.
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