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 A have been collected on a synchrotron radiation source. Crystals belong to space group I4132 with unit-cell dimensions a = b = c = 165.1 A. The crystals are estimated to contain one protein monomer per asymmetric unit, with 55% solvent content.
Klimenko
D E
DE
Astbury Centre for Structural Molecular Biology and School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, England.
Convery
M A
MA
Rowsell
S
S
Thomas
C D
CD
Phillips
S E
SE
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry / Q000235:genetics; D004270:DNA, Circular / Q000737:chemistry / Q000235:genetics; D004268:DNA-Binding Proteins; D010957:Plasmids / Q000737:chemistry; D011487:Protein Conformation; D013211:Staphylococcus aureus / Q000737:chemistry; D015534:Trans-Activators / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D004270:DNA, Circular; D004268:DNA-Binding Proteins; C043650:RepC protein, Staphylococcus aureus; C058757:RepD protein, Staphylococcus aureus; D015534:Trans-Activators; C045264:replication initiator protein; D004265:DNA Helicases