Crystallization and preliminary X-ray crystallographic studies of RepDC, a hybrid rolling-circle plasmid replication initiator protein
The hybrid plasmid‐replication initiator protein RepDC, which is a fusion of the catalytic fragment of the RepD protein and the DNA‐binding fragment of the RepC protein from Staphylococcus aureus, has been successfully crystallized and X‐ray data to 3.5 Å have been collected on a synchrotron radiati...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-05, Vol.55 (5), p.1076-1078 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The hybrid plasmid‐replication initiator protein RepDC, which is a fusion of the catalytic fragment of the RepD protein and the DNA‐binding fragment of the RepC protein from Staphylococcus aureus, has been successfully crystallized and X‐ray data to 3.5 Å have been collected on a synchrotron radiation source. Crystals belong to space group I4132 with unit‐cell dimensions a = b = c = 165.1 Å. The crystals are estimated to contain one protein monomer per asymmetric unit, with 55% solvent content. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444999003005 |