Structure of southern bean mosaic virus at 2.8 Å resolution

Abad‐Zapatero, Celerino; Abdei-Meguid, Sherin S.; Johnson, John E.; Leslie, Andrew G. W.; Rayment, Ivan; Rossmann, Michael G.; Suck, Dietrich; Tsukihara, Tomitake

doi:10.1142/9789814513357_0019

Cited by 8 publications

(11 citation statements)

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“…The structure of the particles of various sobemoviruses (SBMV, SCPMV, SeMV, RYMV, CoMV, and RGMoV) have been determined (Abad-Zapatero et al, 1980;Silva and Rossmann, 1987;Bhuvaneshwari et al, 1995;Opalka et al, 2000;Qu et al, 2000;Tars et al, 2003;Plevka et al, 2007). All these sobemoviruses have the same basic structure with the particles comprising 180 CP subunits which have the canonical β-barrel structure (Figure 3.22).…”

Section: Structure Of Sobemovirusesmentioning

confidence: 99%

Architecture and Assembly of Virus Particles

Hull

2014

Plant Virology

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Section: Structure Of Sobemovirusesmentioning

confidence: 99%

Architecture and Assembly of Virus Particles

Hull

2014

Plant Virology

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“…SBMV is a T = 3 RNA virus with a β-barrel fold in the capsid protein subunit, with marked differences in the long polypeptide termini and protruding loops when compared with the structure of HRV14 major capsid proteins. [30] To reduce the accuracy of the initial phase angles, model phases were calculated from only the Cα coordinates, which is a very crude approximation of the true structure. A hollow sphere was used as the envelope encompassing the virus particle, and a wedge was selected to define the non-crystallographic asymmetric unit.…”

Section: X-ray Diffraction Methods Of Virus Crystalsmentioning

confidence: 99%

Single crystal X-ray diffraction analysis of virus structure and its applications in the development of pharmaceutical agents

Luo

2014

Crystallography Reviews

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To cite this article: Ming Luo (2015) Single crystal X-ray diffraction analysis of virus structure and its applications in the development of pharmaceutical agents, Crystallography Reviews, 21:1-2, 103-121, Virus particles are among the biological subjects that were first found to form single crystals. Their atomic structures were solved when X-ray sources became stronger in intensity. Virus crystals have large unit cell dimensions and are generally sensitive to X-ray radiation. However, the high symmetry of virus particles allows the crystal structure to be solved by non-crystallographic symmetry averaging of electron densities using only the Bragg reflection intensities. Virus crystal structures have expanded our understanding of the principles of virus assembly, recognition of the host receptor, and virus escape from the surveillance of the human immune system. Spherical virus particles are assembled from common capsid subunits and whose layout follows icosahedral symmetry. Interatomic interactions among the capsid protein subunits, especially through their extended termini and loops, stabilize the viral protein shell to encapsulate the viral genome. Conserved folds are found in the protein capsid subunits, such as the β-barrel fold initially observed in the small RNA viruses. These various viral molecular properties and overall layout have been exploited in the design of antiviral pharmaceutical compounds.

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“…[66] The final multiple isomorphous replacement map was greatly improved by means of 10-fold averaging. [67] However, Steve Harrison, working on TBSV, had arrived at a near-atomic resolution structure of the first icosahedral virus, namely TBSV, two years earlier. [23] Both TBSV and SBMV had T = 3 quasi-symmetry (see Section 2 for an explanation of the triangulation number, T).…”

Section: Small Rna Plant Virusesmentioning

confidence: 99%

Virus crystallography and structural virology: a personal perspective

Rossmann

2014

Crystallography Reviews

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My first experiences with crystallography were as a graduate student at the University of Glasgow determining the structure of aromatic hydrocarbons using only primitive hand calculation techniques. I had my first experience using electronic computers as a post-doc in the lab of William Lipscomb in Minnesota. That gave me a good preparation for the structure determination of haemoglobin with Max Perutz in Cambridge. The discovery of the conserved globin fold had a major impact on my subsequent activities. It also provided the foundation for the development of the molecular replacement method and non-crystallographic symmetry electron density averaging that was essential for the structure determination of simple icosahedral viruses. The structure determination of a common cold virus was also a major stimulus for the study of more complex viruses and the development of the use of cryoelectron microscopy. This provided the basis for the investigation of lipid-enveloped viruses such as Sindbis virus and dengue virus. It also provided the technology for the study of bacteriophage DNA packaging motors and the mechanisms of infection by tailed and untailed phages. Downloaded by [University of Connecticut] at 02:51 03 February 2015 58 M.G. Rossmann The beginnings of protein crystallographyThe most common types of crystals encountered in daily life are primarily inorganic substances such as common salt and minerals. Thus, it is not surprising that these substances were the first to be analysed in the first decade or two after the discovery of X-ray diffraction in 1912 by P. Ewald and M. von Laue in Germany and by W.H. Bragg and W.L. Bragg in England. This was most fortunate because many of these structures could be described in terms of a few atoms sitting at special positions on symmetry axes. Even so, it took a great deal of ingenuity and talent to solve these early structures as represented dramatically in the writings of C.P. Snow.[1] Gradually, with increasing experience, crystalized organic substances became within technical range. Kathleen Lonsdale, working in London, determined the structure of some benzene derivatives in 1929 and verified what chemists had suspected, that a benzene ring is planar.[2] The complexity of structures being determined increased steadily. This was aided by the introduction of Fourier syntheses by W.L. Bragg,[3] of the heavy-atom method by J.M. Robertson [4,5] and by the F 2 function by A.L. Patterson.[6] Initially, most organic structures were limited to the analysis of only the principal projections because of the large and tedious experimental procedures and the large computational tasks. Various time-saving devices had been introduced both for collecting data, such as the Weissenbeg camera, and for the computational tasks, such as Beevers-Lipson strips.[7] The power of crystallography was being demonstrated more and more in the 1930s by, for instance, J. Desmond Bernal, Dorothy Crowfoot Hodgkin and Isidor Fankuchen [8] in their work on steroids and by Dorothy Crowfoot Hodgkin in the ...

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Structure of southern bean mosaic virus at 2.8 Å resolution

Cited by 8 publications

References 0 publications

Architecture and Assembly of Virus Particles

Architecture and Assembly of Virus Particles

Single crystal X-ray diffraction analysis of virus structure and its applications in the development of pharmaceutical agents

Virus crystallography and structural virology: a personal perspective

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