Biological membranes represent a unique environment in which integral membrane proteins (MPs) fold to perform diverse biological functions. In many cases, lipids support the native conformation or mediate important interactions between MPs. It is therefore imperative to develop methods that maintain this support for the structural and functional analyses of an exceedingly important class of biological macromolecules. Bicelles are detergent-stabilized phospholipid bilayer discs into which MPs can be reconstituted for biophysical studies. Here, we review recent advances and emerging concepts in employing bicelles for the crystallization and structure determination of MPs. We discuss variations of established procedures as well as alternative approaches, and we present a summary and analysis of the conditions used for bicelle-mediated MP crystallization.