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Título: | X-ray crystallography of viruses |
Autor: | Verdaguer, Núria CSIC ORCID ; Garriga, Damià CSIC ORCID; Fita, Ignacio CSIC ORCID | Palabras clave: | Non-crystallographic symmetry Molecular replacement Virus capsid Phase problem Structural virology Virus X-ray crystallography |
Fecha de publicación: | 2013 | Editor: | Springer Nature | Citación: | Structure and Physics of Viruses: An Integrated Textbook 117-144 (2013) | Resumen: | For about 30 years X-ray crystallography has been by far the most powerful approach for determining virus structures at close to atomic resolutions. Information provided by these studies has deeply and extensively enriched and shaped our vision of the virus world. In turn, the ever increasing complexity and size of the virus structures being investigated have constituted a major driving force for methodological and conceptual developments in X-ray macromolecular crystallography. Landmarks of new virus structures determinations, such as the ones from the first animal viruses or from the first membrane-containing viruses, have often been associated to methodological breakthroughs in X-ray crystallography. In this chapter we present the common ground of proteins and virus crystallography with an emphasis in the peculiarities of virus studies. For example, the solution of the phase problem, a central issue in X-ray diffraction, has benefited enormously from the presence of non-crystallographic symmetry in virus crystals. | Descripción: | Capítulo 4 en la obra, Mateu, Mauricio G. (ed.). Structure and Physics of Viruses: An Integrated Textbook. [S.l.]: Springer, 2013, p.117-144. (Subcellular Biochemistry ; 68) | Versión del editor: | http://dx.doi.org/10.1007/978-94-007-6552-8_4 | URI: | http://hdl.handle.net/10261/110235 | DOI: | 10.1007/978-94-007-6552-8_4 | Identificadores: | doi: 10.1007/978-94-007-6552-8_4 |
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