Preliminary crystallographic analysis of two hypothetical ribose-5-phosphate isomerases from Streptococcus mutans

Two hypothetical ribose-5-phosphate isomerases from S. mutans have been produced in E. coli and crystallized. The crystals diffracted to high resolutions suitable for crystallographic analyses.

Complex of myoglobin with phenol bound in a proximal cavity

The structure of a complex of sperm whale myoglobin with phenol places this inhibitor of the haloperoxidase activity in a proximal cavity that is unlikely to be the halophenol binding site. The absence of phenol binding at the heme edge, where dehalogenation is likely to take place, indicates that the inhibitor and the halophenol substrates only bind in the active site in the presence of hydrogen peroxide.