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Comparison of the 2.45 Å resolution crystal structure of homotrimeric RipC, a putative citrate lyase β subunit from Y. pestis, with structural homologs reveals conserved RipC residues that are implicated in CoA binding.

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Crystal structures of the LpxA protein from A. baumannii were solved in apo forms that were suitable for structure-based antibacterial drug discovery.
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