{Reference Type}: Journal Article
{Title}: Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin.
{Author}: Buts L;Loris R;De Genst E;Oscarson S;Lahmann M;Messens J;Brosens E;Wyns L;De Greve H;Bouckaert J;
{Journal}: Acta Crystallogr D Biol Crystallogr
{Volume}: 59
{Issue}: 0
{Year}: Jun 2003
暂无{DOI}: 10.1107/s0907444903007170
{Abstract}: The Escherichia coli adhesin F17-G is a carbohydrate-binding protein that allows the bacterium to attach to the intestinal epithelium of young ruminants. The structure of the 17 kDa lectin domain of F17-G was determined using the anomalous dispersion signal of a selenium-containing analogue of the monosaccharide ligand N-acetyl-d-glucosamine in which the anomeric oxygen was replaced by an Se atom. A three-wavelength MAD data set yielded good experimental phases to 2.6 A resolution. The structure was refined to 1.75 A resolution and was used to solve the structures of the ligand-free protein and the F17-G-N-acetyl-d-glucosamine complex. This selenium-carbohydrate phasing method could be of general use for determining the structures of carbohydrate-binding proteins.