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Abstract:
I. INTRODUCTION
Membrane proteins still present a major challenge in structural biology. Electron microscopy (EM) of two-dimensional (2D) crystals is an increasingly important technique for studying their structure and function. An earlier review (Kühlbrandt, 1992) published about 10 years ago outlines the basic techniques and concepts. While these 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. Recent technical developments are also discussed in this chapter and may help to facilitate the future production of 2D crystals. Several other reviews published in the past 10 years (Jap et al., 1992; Mosser, 2001; Rigaud et al., 2000; Walz and Grigorieff, 1998) address various aspects of 2D crystallisation.
