Another interest of my group are very high resolution (1.0 Å or better) structures of phosphate binding protein. These studies require synchrotron-generated X-rays of very high brilliance. Atomic structures at this resolution are able to reveal details of hydrogen bonding that cannot be obtained by other methods.

Shown is a very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

Also shown is Trp156 electron density, clearly showing the individual carbon bulges allowing for its unmistakable identification.

Shown here is a tyrosine's electron density.

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.Wang Z, Luecke H, Yao N, Quiocho FA (1997) Nat. Struct. Biol. 4(7):519-522 (abstract)

High specificity of a phosphate transport protein determined by hydrogen bonds. Luecke H, Quiocho FA (1990) Nature 347(6291):402-406 (abstract)

This page created 8/8/98 by JP, last modified 2/25/2000.