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Crystallization and preliminary X-ray diffraction analysis of West Nile virus
Autoři | |
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Rok publikování | 2010 |
Druh | Článek v odborném periodiku |
Časopis / Zdroj | Acta crystallographica. Section F Structural biology and crystallization communications |
Fakulta / Pracoviště MU | |
Citace | |
Doi | http://dx.doi.org/10.1107/S1744309110009899 |
Obor | Biochemie |
Klíčová slova | DENGUE VIRUS; ENVELOPE GLYCOPROTEIN; MEMBRANE-FUSION; VAPOR-DIFFUSION; PROTEIN; MATURATION; CRYSTALS |
Popis | West Nile virus, a human pathogen, is closely related to other medically important flaviviruses of global impact such as dengue virus. The infectious virus was purified from cell culture using polyethylene glycol (PEG) precipitation and density-gradient centrifugation. Thin amorphously shaped crystals of the lipid-enveloped virus were grown in quartz capillaries equilibrated by vapor diffusion. Crystal diffraction extended at best to a resolution of about 25 angstrom using synchrotron radiation. A preliminary analysis of the diffraction images indicated that the crystals had unit-cell parameters a similar or equal to b similar or equal to 480 angstrom, gamma = 120 degrees, suggesting a tight hexagonal packing of one virus particle per unit cell. |