I am interested in improving membrane protein crystallization methods to produce high quality crystals essential for structure determination. Compared to thousands of soluble proteins, the Protein Data Base (PDB) has around one hundred deposited membrane protein structures. Therefore, it is obvious that existing crystallization methods are not sufficient and further improvements are needed. During high-throughput crystallization screens, the membrane protein solubilized in flexible detergent micelle causes most difficulties to achieve high quality crystals. The micelles initiate random packing of protein molecules leading to poor quality crystals. As a remedy, we are working on attaching hydrophilic polyethylene glycols site specifically to the hydrophobic backbone of the protein, which will result in higher water solubility and stability leaning towards crystallizing membrane proteins in soap (detergent) free environment.