Unusual diffraction of type B influenza virus neuraminidase crystals.
An unusual X-ray diffraction pattern by tetragonal crystals of a type B influenza virus neuraminidase was observed in that the odd-l reflections were missing or diffuse while the even-l reflections were sharp and strong. A statistical analysis showed that an error (epsilon) in the spacing of successive planes of neuraminidase molecules was randomly distributed along the c direction, which resulted in such an unusual diffraction pattern. The error epsilon follows the Bernoullian distribution and may be caused by a flexible loop on the top surface of the neuraminidase.
Luo
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Center for Macromolecular Crystallography, University of Alabama, Birmingham 35294.
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D009981:Influenza B virus / Q000201:enzymology*; D046911:Macromolecular Substances; D008433:Mathematics; D008961:Models, Structural; D009439:Neuraminidase / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods
D046911:Macromolecular Substances; D009439:Neuraminidase