Atomic‐resolution crystal structure of the antiviral lectin scytovirin

The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single‐wavelength anomalous scattering and refined with data extending to 1.3 Å and 1.0 Å resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost...

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Veröffentlicht in:	Protein Science 2007-12, Vol.16 (12), p.2756-2760
Hauptverfasser:	Moulaei, Tinoush, Botos, Istvan, Ziółkowska, Natasza E., Bokesch, Heidi R., Krumpe, Lauren R., McKee, Tawnya C., O'Keefe, Barry R., Dauter, Zbigniew, Wlodawer, Alexander
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence AMINO ACIDS anomalous scattering ATOMS Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification BONDING Carrier Proteins - chemistry Carrier Proteins - isolation & purification CHAINS CRYSTAL STRUCTURE Crystallography, X-Ray Cyanobacteria - chemistry DISULFIDES LECTINS Lectins - chemistry Lectins - isolation & purification MASS SPECTROSCOPY MATERIALS SCIENCE Models, Molecular Molecular Sequence Data national synchrotron light source new fold Protein Conformation Protein Structure Report Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification RESOLUTION SCATTERING scytovirin
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