G-protein coupled receptors (GPCRs) represent the largest group of integral membrane proteins, accounting for over 50% of all pharmaceuticals targets. However, GPCRs prove difficult to study due to problems with their expression, purification, and stability outside of the membrane environment. GPCRs, as with all membrane proteins, require surfactants to stabilize their conformation outside the plasma membrane. High-level expression and purification of the human adenosine A2a (hA2aR) receptor in a heterologous yeast system has enabled the characterization of this receptor through biophysical techniques. Here, we assess the ability of different surfactants to stabilize the human adenosine A2a (A2aR) receptor, as measured through ligand binding and biophysical methods. After solubilization from the yeast membrane in n-dodecyl-beta-D-maltoside, different surfactants including maltosides, thiomaltosides, and glucosides were exchanged and the effects of this exchange on the protein detergent complex (PDC) were carefully monitored. The addition of a mammalian cholesterol analog (CHS) to the PDC is found to be crucial to the maintenance of proper structure of A2aR. This interaction may hold the 7-alpha helical domains of the GPCR more rigid, in an active conformation within the micelle. Furthermore, surfactants which share common structure and differ only by one carbon length show marked differences in the ability to stabilize hA2aR. We will further explore the effects of surfactant type, chain length, and other parameters on the activity of purified A2aR and on the protein detergent complex.