Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase.
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Burmeister WP, Daniels RS, Dayan S, Gagnon J, Cusack S, Ruigrok RW
Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase.
Virology. 1991 Jan;180(1):266-72.
- PubMed ID
- 1984652 [ View in PubMed]
- Abstract
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%.