Crystallographic studies of bacterial single-stranded DNA-binding proteins
Single-stranded DNA-binding proteins (SSBs) from different bacteria ( E.coli, B. abortus, P. mirabilis and S. marcenecens) were crystallised and their structures determined by X-ray crystallography. The overall topology of all four SSB structures are similar. The important residues His-55, which is involved in tetramerization, Trp-40, Trp-54, Trp-88 and Phe-60, which are involved in ssDNA-binding, are sequentially, structurally and conformationally conserved. The four structures do however, show difference in and near their loop regions. Two new cryo-cooling techniques are described. They have been shown to work favorably for SSBs and several other proteins.