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Abstract:
During the past year, structural biologists have reaped a wealth of new information concerning the molecular organization of membrane proteins at low and high resolution by employing both electron and X-ray approaches. There have been no fewer than five X-ray structures: the KesA potassium channel [I], a mechanosensitive channel and three outer membrane ß-barrel proteins, all from bacteria. Electron crystallography of Two-dimensional crystals has provided the phases for the recent high-resolution structures of bacteriorhodopsin and has yielded interesting insights into the structures of several other membrane proteins at intermediate resolution. Finally, electron cryomicroscopy and image processing of single particles have provided important information about a large membrane protein complex. Descriptions of many of these developments and their implications for future studies are covered in this current section.
