Bibliographic Citation
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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 Date | 1991 Jan 01 |
OSTI Identifier | OSTI ID: 6152500 |
Other Number(s) | ISSN0042-6822; CODEN: VIRLA |
Resource Type | Journal Article |
Resource Relation | Virology ; Vol/Issue: 180:1; Databank sent to: GENBANK/M54967 |
Subject | 550201 -- Biochemistry-- Tracer Techniques; O-GLYCOSYL HYDROLASES-- AMINO ACID SEQUENCE; ELECTRON MICROPROBE ANALYSIS;ELECTROPHORESIS;ENZYME ACTIVITY;GENES;INFLUENZA VIRUSES |
Related Subject | CHEMICAL 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 Publication | United States |
Language | English |
Format | Pages: 266-272 |
System Entry Date | 2001 May 13 |
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