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The crystal structure of the S. aureus amidohydrolase SACOL0085 reveals that a conserved cysteine residue at the active site serves as a bidentate ligand coordinating two Mn2+ ions.

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The cloning, purification, crystallization and preliminary X-ray diffraction studies of S. aureus homoserine dehydrogenase, an enzyme that regulates the biosynthesis of several essential amino acids, are reported.
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