Stuctural studies on human erythrocyte BAND-3

人红细胞阴离子交换剂AE1，也被称为带3，允许碳酸氢盐穿过红细胞膜以交换氯。这是允许血液将大量碳酸盐输送到肺部的重要过程。带3也与许多人类疾病状态有关。为了了解该蛋白的确切作用机制和揭示这些疾病状态的进一步细节，有必要获得人类形式的Band 3膜结构域的精确结构信息。对此最合适的技术是x射线晶体学。人类膜蛋白的结构测定是极具挑战性的，因为没有x射线结构被解决。到目前为止，已经有可能从人类红细胞中获得高纯度的带3蛋白，并产生晶体。然而，从晶体的x射线分析中获得的数据质量不足以解决结构问题。本应用侧重于优化带3晶体，以获得适合于结构确定的高质量数据。

The Human Erythrocyte Anion exchanger, AE1, also known as Band 3, allows bicarbonate to cross the red blood cell membrane in exchange for chloride. This is an essential process in allowing the bloodstream to transport large quantities of carbonate to the lungs. Band 3 is also associated with a number of human disease states. In order to understand the precise mechanism of action of the protein and reveal further details on these disease states it is necessary to obtain precise structural information for the human form of Band 3 membrane domain. The most suitable technique for this is X-ray crystallography. The structure determination of human membrane proteins is extremely challenging as evidenced by the fact that no X-ray structure has been solved. So far it has been possible to obtain highly pure Band 3 protein from human red blood cells which has yielded crystals. However the data obtained from the X-ray analysis of the crystals is not of sufficient quality to solve the structure. This application focuses on the optimisation of the Band 3 crystals in order to obtain high quality data suitable for structure determination.