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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 9 (1993), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have examined the surface topography and channel connectivity of a naturally crystalline porin that is known to be functional, and whose structure has not been perturbed by detergent extraction, A three-dimensional density map, calculated from two independent tilt series of negatively stained cell envelopes, reveals three separate channels per trimer on one side (the ‘smooth’ side), and a single common opening at the other (‘rough’) side. This arrangement is consistent with the molecular structures recently determined at high resolution by X-ray crystallography for three other porins after detergent solubilization, and implies that the Bordetella pertussis porin may have the same kind of folding. Surface relief maps calculated from electron micrographs of cell envelopes contrasted by unidirectional shadowing clearly show that the side with single opening (i.e. the rough side) represents the external surface.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The core antigen (HBcAg) assembles into capsids of twoo sizes, with icosahedral triangulation numbers of T = 3 (280 Å diameter, 90 dimers), and T = 4 (310 A, 120 dimers), respectively3'4. The most detailed structural information to date has emerged from cryo-electron microscopy at ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 475-495 
    ISSN: 0091-7419
    Keywords: T4 giant phage ; morphogenesis ; optical/computer image processing ; protein composition ; phage capsid structure ; phage head length determination ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A study has been made of the structure of the capsids of T4D giant phage produced from mutants in gene 23 and temperature-sensitive mutants in gene 24, and T4D and T2L giant phage formed by the addition of L-canavanine followed by an L-arginine chase in the growth medium.All the giant phage capsids have been shown to be built according to the same geometrical architecture. This consists of a near-hexsagonal surface net, lattice constant 129.5 Å, folded into a left-hand T = 13 prolate icosahedron elongated along one of its fivefold symmetry axes. Their only apparent difference from wild-type T-even phage capsids is their abnormally elongated tubular part.A comparison of the capsomere morphologies and protein compositions of the giant phage capsids showed that all T4D giants are indentical but differ from T2L: The T4D capsomere has a complex (6+6+1)-type morphology, whereas the T2L has a simple 6-type. T2L phage, however, lack two capsid proteins, “soc” and “hoc”, present in T4D. The difference in capsomere morphology can therefore be related to the difference in the protein compositions of these two phage.Possible differences between the initiation and means of length regulation of giant phage heads and the aberrant polyheads are discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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