Three-Dimensional Structure of an Olefinic Enzyme Pathway Through X-Ray Crystallography
Antibiotic resistance is a serious problem of the modern world, which is predicted to only get worse. One of the main issues with resistance is the ability of bacteria to target a fundamental part of an antibiotic class and essentially gain resistance to many drugs simultaneously. Here, we attempted to characterize the structure of OleA, the first enzyme in a biosynthetic line capable of creating a β-lactone ring through X- ray crystallography. We have shown OleA to be a hydrophobic enzyme, requiring detergents for crystallization. Additionally, presence of polyethylene glycols in a slightly basic pH seem to favor crystallization. Further experiments can narrow down the required conditions for proper protein crystallization, which allows the structure to be solved through X-ray crystallography.