The crystallization of membrane proteins is an essential technique for the determination of atomic models of three-dimensional structures by X-ray crystallography. The compositions of solutions of purified membrane proteins are altered, so as to transiently induce supersaturation, a requirement for crystal nucleation and growth. The establishment of the precise optimal crystallization conditions has to be performed individually by a combination of systematic approaches and trial-and-error. These procedures have become more efficient due to the introduction of laboratory automation. Here we describe the crystallization of the dihaem-containing quinol:fumarate reductase (QFR) membrane protein complex and illustrate key factors important in the screening process.