Abstract
Membrane proteins still present a major challenge in structural biology. Electron microscopy (EM) of 2D crystals is an increasingly important technique for studying their structure and function. While the basic techniques and concepts are unchanged and valid, the number of membrane proteins crystallized in 2D has risen encouragingly in the past three or four years, no doubt largely due to the recent progress in expressing membrane proteins in homologous or heterologous systems. The evaluation of more than 60 2D crystallization protocols now provides a sound base for some general guidelines. This chapter discusses recent technical developments, which may help to facilitate the future production of 2D crystals. Several other reviews published in the past 10 years address various aspects of 2D crystallisation.
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