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Zusammenfassung:
High-resolution electron crystallography is emerging as an alternative to X-ray crystallography for determining the structure of biological macromolecules at near-atomic resolution. The technique combines electron diffraction, high-resolution electron microscopy and image processing. Crystals for electron crystallography need to be very thin. Crystalline monolayers, often referred to as two-dimensional crystals, are ideal. With membrane proteins, order in two dimensions may be easier to achieve than in three dimensions. Indeed, many membrane proteins tend to form two-dimensional crystals. A well-known example is bacteriorhodopsin which occurs naturally in highly ordered two-dimensional arrays. Two-dimensional crystals can also be grown from purified detergent-solubilized membrane proteins, as is the case with the light-harvesting chlorophyll a/b-protein complex (LHC-II) (3) and bacterial porins
