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Figure 2
Schematic representation of the workflow of virus structure determination in EM, SAXS and X-ray crystallography. The black arrow at the top indicates the band corresponding to the virus particles following ultracentrifugation. In EM the purified virus is placed on a microscopy grid, flash-cooled and the two-dimensional projections of the virus are then visualized in an electron microscope, producing real-space images (top); post-processing of these images provide the virus structure (bottom). In SAXS the purified virus in solution is irradiated by an X-ray beam producing a low-angle scattering curve (top) containing raw data in reciprocal space; post-processing of the data produces the overall shape and molecular architecture (bottom) of the virus. In X-ray crystallography the purified virus is used to obtain virus crystals (top) that are irradiated to produce diffraction images (centre) containing raw data in reciprocal space; once the data have been processed and the phase-problem has been solved, the virus structure is obtained at atomic resolution (bottom). The outlined region in the virus models across the EM, SAXS and X-ray panels delineates one of the 20 viral facets and the numbers indicate the icosahedral symmetry axes (2, twofold; 3, threefold; 5, fivefold). Each technique provides structural information in a different resolution range, at times overlapping. Reproduced from Badia-Martinez et al. (2013BB9) with kind permission from Springer Science+Business Media BV.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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