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  • 1
    ISSN: 1432-072X
    Keywords: Chroomonas ; Cryptomonad biliprotein ; Crystallization ; Phycocyanin-645 ; Protein crystallography ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The water-soluble antenna chromoprotein phycocyanin-645 from a Chroomonas species (Cryptophyceae) has been crystallized. X-ray precession photographs prove space groups P3121 (or the enantiomorphic P3221) for the trigonal and P212121 for the orthorhombic crystals. Density measurements indicate that the asymmetric units of these crystals contain three or two heterotetrameric units (αάβ 2), respectively. The packing of both crystal forms is quite different to that of any other crystals reported so far for phycobiliproteins of blue-green and red algae. The cationic detergent benzalkonium chloride (BAC) is strongly bound in the crystals. Both observations indicate a considerable membrane affinity and a unique association behaviour of the phycobiliproteins from cryptomonads.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0570-0833
    Keywords: Bacterial flagella ; Proteins ; Flagellin ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In comparison with the relatively complicated flagella of all nucleated organisms, most of the actively motile bacteria have very much simpler locomotion organelles. These flagella are long thin filaments with a helical superstructure, anchored at one end in the cell membrane. Helical waves pass along the flagella in the distal direction during locomotion. In the flagella, identical structural units of a single protein species, flagellin, are linked to one another by non-covalent bonds. The flagellin subunits can be separated from one another by mild methods, and their biochemistry as well as their structure and morphology can be investigated in the isolated state. Under certain conditions they can reaggregate in vitro to form polymorphous helical filaments, which are practically indistinguishable from intact flagella. In the flagellum, the elongated flagellin molecules have a layered arrangement in about ten parallel strands, which in turn form a hollow cylinder. Since this cylinder is deformed into a large helix, the individual chemically identical flagellin protomers and the protomer strands in the helical flagella are only quasi-equivalent. The conformation and bonding pattern of the individual longitudinal flagellin lines can presumably be controlled in vitro by the basal structures, so that movement within the flagellum could conceivably occur as follows. A cyclically induced change in the length of the individual strands could result in an apparent rotation of the helical flagellum. According to hydrodynamic calculations, the resulting forward thrust is sufficient to propel the bacteria at the observed speeds of up to 50 μm/s.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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