CRYSTALLOGRAPHIC STRUCTURE DETERMINATION OF SYNECHOCYSTIS HEMOGLOBIN PCC 6803

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。截短血红蛋白（trHb）是一个新发现的血红蛋白家族，与典型的3-on-3珠蛋白折叠相比，具有以前未见过的2-on-2珠蛋白折叠，导致许多结构和机制差异。集胞藻血红蛋白PCC 6803（SynHb）是一种具有独特配体结合动力学的trHb。已经使用了折射率为1.8埃的SynHb晶体来获得天然数据集，并将用于MAD定相，这是由于缺乏分子置换模型所必需的。SynHb晶体结构的测定将提供第一个非配体结合，六配位trHb。这将有助于阐明远端残基之间的复杂相互作用，并提供更多的信息，一般的SynHb和trHbs的配体结合特性。

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.