Stuctural studies on human erythrocyte BAND-3

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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.