Abstract
Complexes of the gene 5 protein from bacteriophage fd with a variety of oligodeoxynucleotides, ranging in length from two to eight and comprised of several different sequences, have been formed and crystallized for X-ray diffraction analysis. The crystallographic parameters of four different unit cells, all of which are based on hexagonal packing arrangements, indicate that the fundamental unit of the complex is composed of six gene 5 protein dimers. We believe this aggregate has 622 point group symmetry and is a ring formed by end-to-end closure of a linear array of six dimers. From our results we have proposed a double-helix model for the gene 5 protein-DNA complex in which the protein forms a spindle or core around which the DNA is spooled. Currently 5.0-A X-ray diffraction data from one of the crystalline complexes is being analyzed by molecular replacement techniques to obtain a direct image of the protein-nucleic acid complex.
Highlights
Complexes ofthe gene 5 protein from bacteriophage fd with a variety of oligodeoxynucleotides, ranging in length from two t o eight and comprised of several different sequences, have been formed and crystallized for X-ray diffraction analysis
5.0-aX-ray diffraction data from one of the crystalline complexes is being analyzed by molecular replacement techniques to obtain a direct image of the protein--nucleic acid complex
The gene 5 protein from fd bacteriophage has proved to be a useful system for such studies since it can be crystallized as a monomer in the absence of nucleic acid [11
Summary
Complexes ofthe gene 5 protein from bacteriophage fd with a variety of oligodeoxynucleotides, ranging in length from two t o eight and comprised of several different sequences, have been formed and crystallized for X-ray diffraction analysis. Determination of the structure of a complex between a DNA binding protein and fragments of nucleic acid by X-ray diffraction analysis promises substantial insight into the means by which these two important macromolecules interact.
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