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
Hauptverfasser: Klimenko, Dmitry E., Convery, Máire A., Rowsell, Siân, Thomas, Christopher D., Phillips, Simon E. V.
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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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999003005