Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus
Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4′‐phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty‐acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipita...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-04, Vol.60 (4), p.773-774 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4′‐phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty‐acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 Å, respectively. Full sets of X‐ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444904003282 |