The surfaces of glass coverslips of the type typically used for protein crystallization were modified with four types of transparent, chemically distinct self-assembled monolayers (SAMs). The SAM-functionalized surfaces exhibit a much higher degree of order and chemical uniformity than silanized glass, as judged by contact angle measurements. These characteristics lead to a marked increase in the range of solution conditions under which large crystals of lysozyme, alpha-lactalbumin, ribonuclease. hemoglobin, thaumatin, and catalase are observed to form. The results are rationalized in terms of a marked reduction in the rate of non-productive nucleation relative to the rate of crystal growth.