Sequence and crystallization of influenza virus b/Beijing/1/87 neuraminidase
Identifieur interne : 002011 ( Main/Exploration ); précédent : 002010; suivant : 002012Sequence and crystallization of influenza virus b/Beijing/1/87 neuraminidase
Auteurs : Wilhelm-Pascal Burmeister [France] ; Rod S. Daniels [Royaume-Uni, France] ; Sonia Dayan [France] ; Jean Gagnonj [Royaume-Uni, France] ; Stephen Cusack [France] ; Rob W. H. Ruigrok [France]Source :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Active site, Amino, Amino acid sequence, Amino acids, Asymmetric unit, Biosystems model, Carbon film, Crystal density, Crystal density measurements, Crystal forms, Density measurements, Grenoble cddex, High resolution, High values, Influenza, Influenza virus, Intact virus, Laver, Lysozyme crystals, Neuraminidase, Neuraminidase gene, Neuraminidase heads, Neuraminidase sequence, Nucleotide, Nucleotide sequence, Phosphate buffer, Precession photograph, Primer, Reading frame, Resolution nature, Room temperature, Sequencing, Skehel, Tetragonal, Tetragonal plates, Trigonal, Trigonal crystals, Trypsin, Trypsin digestion, Virus.
Abstract
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%.
Url:
DOI: 10.1016/0042-6822(91)90031-6
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">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%.</div>
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