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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase.

Influenza B/Beijing/1/87 neuraminidase heads were isolated from virus via trypsin digestion and characterized by PAGE, N-terminal sequencing, electron microscopy, and enzyme activity. The heads were crystallized into two crystal forms; tetragonal plates, like other neuraminidase crystals described before, that diffract to medium resolution (3 A) and a new form consisting of trigonal prisms or needles that diffract to high resolution (at least 2 A). The gene segment coding for neuraminidase was sequenced and compared with the neuraminidase sequence of B/Lee/40. The deduced amino acid sequences for neuraminidase showed only a 7% difference, whereas those for the NB proteins differed by 20%.[1]

References

  1. Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase. Burmeister, W.P., Daniels, R.S., Dayan, S., Gagnon, J., Cusack, S., Ruigrok, R.W. Virology (1991) [Pubmed]
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