PMID:10089419
| Citation |
Hargreaves, D, Rafferty, JB, Sedelnikova, SE, Lloyd, RG and Rice, DW (1999) Crystallization of Escherichia coli RuvA complexed with a synthetic Holliday junction. Acta Crystallogr. D Biol. Crystallogr. 55:263-5 |
|---|---|
| Abstract |
During homologous recombination in Escherichia coli the RuvA, B and C proteins interact specifically with the Holliday junction formed by the action of RecA to promote the strand-exchange reaction. RuvA, a homotetrameric protein of molecular weight 88 kDa, has been overexpressed in E. coli, purified and co-crystallized with a synthetic Holliday junction substrate made from four 18-base deoxyoligonucleotides. Crystals were grown using the hanging-drop vapour-diffusion method with sodium acetate as the precipitant. The crystals diffract to a resolution of 6 A and belong to the monoclinic system, space group C2, with cell parameters a = 148, b = 148, c = 106 A and beta = 123 degrees. The X-ray analysis of these crystals should reveal the structure of the Holliday junction and its mode of binding to RuvA, providing new insights into the molecular mechanism of genetic recombination. |
| Links |
PubMed Online version:10.1107/S0907444998006672 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Base Sequence; Crystallization; DNA Helicases; DNA, Bacterial/chemistry; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/isolation & purification; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; Protein Conformation; Recombination, Genetic; X-Ray Diffraction |
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