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%.
Burmeister
W P
WP
EMBL Grenoble Outstation c/o ILL, France.
Daniels
R S
RS
Dayan
S
S
Gagnon
J
J
Cusack
S
S
Ruigrok
R W
RW
D000595:Amino Acid Sequence; D001483:Base Sequence; D003460:Crystallization; D004279:DNA, Viral / Q000235:genetics; D004577:Electron Probe Microanalysis; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D009981:Influenza B virus / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000235:genetics* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D004279:DNA, Viral; D009439:Neuraminidase