CRYSTALLOGRAPHIC ANALYSIS OF FERRIC IRON BINDING PROTEIN BY MAD

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Multiwavelength anomalous dispersion (MAD) data using anomalous scattering from selenium and iron will be used to determine the structure of ferric iron binding protein (FBP) from Haemophilus influenzae. This protein is vital to several pathogenic bacteria and is a promising target of structure-based drug design. Attempts to determine the crystal structure by traditional methods have been extremely frustrating. Very strong anomalous scattering from the iron atom along with incorporated seleno-methionine will make this an ideal candidate for MAD phasing. The crystals diffract to 1.6 E resolution.