Membrane protein structure biology is one of the rapidly growing fields in biosciences. Lots of research has been done in the field of membrane crystallization. Though a vast number of proteins have been studied and the structure known, some of the protein targets are immune o traditional approach to membrane protein crystallization with detergents. This has given rise to the emergence of lipidic phase crystallization which includes lipidic cubic phase and bicelle crystallization methods.
These new methods help in crystallizing membrane proteins by long term structural stability and there by proper crystallization. As the only reliable way to assess the structure of any protein is crystallography, technology is rapidly growing to refine the crystallization process for immune membrane proteins click here.
Diffraction at high resolution when obtaining crystals of membrane proteins remains the great stumbling block in membrane protein structure determination. Crystallizing membrane proteins from a bicelle lipid/detergent mixture is a new method in protein crystallization. Protein structure determination with the help of bicelle is flexible and simple.
Bicelles are just disk-like micelles, formed by mixing phosphatidylcholine lipid such as Dimyristoyl-phosphatidylcholine (DMPC) and a detergent such as 3-[(3- cholamidopropyl) dimethylammonio]-2-hydroxy-1-propanesulfonate (CHAPSO). The bicelle discs can be described as patches of lipid bilayers with detergent molecules lining the apolar edges of each bilayer. Bicelles present a compromise between a rigid lipidic medium and an artificial detergent medium while offering beneficial aspects from both. Membrane proteins can be readily reconstituted into bicelles and are maintained in a native-like bilayer environment, which can be manipulated with almost the same ease as detergent solubilized membrane proteins, making it compatible with standard high-throughput screening.
There are many membrane protein structure tools are available in the market for the research of bicelle crystallization with which one can successfully crystallize membrane proteins and determine protein structure. Recently, a significant number of membrane proteins have been successfully crystallized using the bicelle method, including Bacteriorhodopsin, ß2 adrenergic receptor/Fab, Voltage-Dependent Anion Channel and Xanthorhodopsin.