Identification of the tailspike protein from the Salmonella newington phage epsilon 34 and partial characterization of its phage-associated properties.


:The lipopolysaccharide (LPS) of the Salmonella cell surface serves as the receptor for a very large number of bacterial viruses. The tailspike protein from these viruses recognizes the LPS as its initial receptor. It is proposed that the study of the P22 and epsilon 34 tailspike proteins could serve as a model for the study of the interaction of proteins with LPS. Toward this end, the tailspike protein of the epsilon 34 phage has been identified. The data suggest similarities between the epsilon 34 tailspike protein and the P22 tailspike protein. Some properties related to the interaction of the phage tailspike with its receptor are reported.


J Struct Biol


Greenberg M,Dunlap J,Villafane R




Has Abstract


1995-11-01 00:00:00














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    journal_title:Journal of structural biology

    pub_type: 杂志文章


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  • Crystallization of sparingly soluble stress-related proteins from cyanobacteria by controlled urea solublization.

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    journal_title:Journal of structural biology

    pub_type: 杂志文章


    authors: Dines M,Sendersky E,Schwarz R,Adir N

    更新日期:2007-04-01 00:00:00

  • Tomo3D 2.0--exploitation of advanced vector extensions (AVX) for 3D reconstruction.

    abstract::Tomo3D is a program for fast tomographic reconstruction on multicore computers. Its high speed stems from code optimization, vectorization with Streaming SIMD Extensions (SSE), multithreading and optimization of disk access. Recently, Advanced Vector eXtensions (AVX) have been introduced in the x86 processor architect...

    journal_title:Journal of structural biology

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    authors: Agulleiro JI,Fernandez JJ

    更新日期:2015-02-01 00:00:00

  • Domains of Importin-alpha2 required for ring canal assembly during Drosophila oogenesis.

    abstract::Null-mutation in Drosophila importin-alpha2, such as the deficiency imp-alpha2(D14), causes recessive female sterility with the formation of dumpless eggs. In imp-alpha2(D14) the transfer of nurse cell components to the oocyte is interrupted and the Kelch protein, an oligomeric ring canal actin organizer, is normally ...

    journal_title:Journal of structural biology

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    authors: Gorjánácz M,Török I,Pomozi I,Garab G,Szlanka T,Kiss I,Mechler BM

    更新日期:2006-04-01 00:00:00

  • The crystallographic structure of Panicum Mosaic Virus (PMV).

    abstract::The structure of Panicum Mosaic Virus (PMV) was determined by X-ray diffraction analysis to 2.9Å resolution. The crystals were of pseudo symmetry F23; the true crystallographic unit cell was of space group P2(1) with a=411.7Å, b=403.9Å and c=412.5Å, with β=89.7°. The asymmetric unit was two entire T=3 virus particles,...

    journal_title:Journal of structural biology

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    authors: Makino DL,Larson SB,McPherson A

    更新日期:2013-01-01 00:00:00

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    abstract::In recent years, cryo-electron microscopy (cryo-EM) has established itself as a key method in structural biology, permitting the structural characterization of large biomolecular complexes in various functional states. The data obtained through single-particle cryo-EM has recently seen a leap in resolution thanks to l...

    journal_title:Journal of structural biology

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    authors: Trabuco LG,Schreiner E,Gumbart J,Hsin J,Villa E,Schulten K

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    journal_title:Journal of structural biology

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    authors: Kryshtafovych A,Adams PD,Lawson CL,Chiu W

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    authors: Greenberg I,Shkolnisky Y

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    authors: Mesman RJ

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    journal_title:Journal of structural biology

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    authors: Eisenstein F,Danev R,Pilhofer M

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  • STEM tomography analysis of the trypanosome transition zone.

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  • Structural and dynamics studies of the TetR family protein, CprB from Streptomyces coelicolor in complex with its biological operator sequence.

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    authors: Bhukya H,Jana AK,Sengupta N,Anand R

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    journal_title:Journal of structural biology

    pub_type: 杂志文章


    authors: Hodgkinson JL,Newman TM,Marston SB,Severs NJ

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    journal_title:Journal of structural biology

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    abstract::Cryo-tomography in the electron microscope is unique in its ability to provide high-resolution, three-dimensional structural information about cells, organelles and macromolecules in a nearly native, frozen-hydrated state. However, the phase-contrast imaging method used in conventional cryo-electron tomography fails t...

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    authors: Madl T,Gabel F,Sattler M

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    pub_type: 杂志文章


    authors: Koch SL,Shriver MD,Jablonski NG

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    journal_title:Journal of structural biology

    pub_type: 杂志文章


    authors: Rich SA,Marko M,Gibbons WE

    更新日期:1992-01-01 00:00:00