CRYSTALLOGRAPHIC STRUCTURE DETERMINATION OF SYNECHOCYSTIS HEMOGLOBIN PCC 6803

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Truncated hemoglobins (trHb) are a newly discovered family of Hbs with a previously unseen 2-on-2 globin fold resulting in many structural and mechanistic differences compared to typical 3-on-3 globin folds. Synechocystis Hemoglobin PCC 6803 (SynHb) is a trHb with unique ligand binding kinetics. SynHb crystals that diffract to 1.8 angstroms have been used to obtain a native data set and will be used for MAD phasing, necessary due to the absence of a model for molecular replacement. Determination of the SynHb crystal structure will provide the first look at a non-ligand bound, hexacoordinate trHb. This will help to elucidate the complex interaction between distal residues, and provide additional information on the ligand binding properties of SynHb and trHbs in general.