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- W49051618 abstract "The use of the small detergent β-D-octylglucopyranoside allowed crystallization of the two integral membrane proteins bacteriorhodopsin and porin by precipitation using salts or polyethylenglycol. The success with this detergent fits well into the working hypothesis that the detergent is still present in the crystals and bound to the hydrophobic protein surface domains with its hydrophopic tail. A further improvement in the crystallization procedure was achieved by the introduction of small amphiphilic molecules like heptane-1,2,3-triol. These small amphiphilic molecules are thought to replace those detergent molecules that are too large to fit perfectly into cavities of the proteins crystal lattice. The small amphiphilic molecules may also change shape and size of the detergent micelles that incorporate the detergent-solubilized protein. Larger polar surface parts of the membrane protein might then be available for polar protein–protein interaction in the crystallization process. The application of this small amphiphile concept has allowed the crystallization of photosynthetic reaction centers from Rhodopseudomonas viridis , a bacteriochlorophyll b containing purple photosynthetic bacterium. The crystals of this membrane protein complex diffract X-rays to at least 2.5 8 resolution. This chapter presents the recent progress in crystallization procedures for membrane proteins and describes the actual state of X-ray structure analysis and protein chemistry of photosynthetic reaction centers." @default.
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- W49051618 date "1983-01-01" @default.
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- W49051618 title "CRYSTALLIZATION OF MEMBRANE PROTEINS AND ACTUAL STATE OF STRUCTURE ANALYSIS OF PHOTOSYNTHETIC REACTION CENTRE CRYSTALS" @default.
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- W49051618 doi "https://doi.org/10.1016/b978-0-444-80540-9.50026-1" @default.
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