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Title Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase
Creator/Author Burmeister, W.P. ; Daniels, R.S. ; Dayan, S. ; Gagnon, J. ; Cusack, S. ; Ruigrok, R.W. (EMBL Grenoble Outstation c/o ILL (France))
Publication Date1991 Jan 01
OSTI IdentifierOSTI ID: 6152500
Other Number(s)ISSN0042-6822; CODEN: VIRLA
Resource TypeJournal Article
Resource RelationVirology ; Vol/Issue: 180:1; Databank sent to: GENBANK/M54967
Subject550201 -- Biochemistry-- Tracer Techniques; O-GLYCOSYL HYDROLASES-- AMINO ACID SEQUENCE; ELECTRON MICROPROBE ANALYSIS;ELECTROPHORESIS;ENZYME ACTIVITY;GENES;INFLUENZA VIRUSES
Related SubjectCHEMICAL ANALYSIS;ENZYMES;GLYCOSYL HYDROLASES;HYDROLASES;MICROANALYSIS;MICROORGANISMS;MOLECULAR STRUCTURE;PARASITES;VIRUSES
Description/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%.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 266-272
System Entry Date2001 May 13

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