Ontology highlight
ABSTRACT:
SUBMITTER: Moulaei T
PROVIDER: S-EPMC2222830 | biostudies-literature | 2007 Dec
REPOSITORIES: biostudies-literature
Moulaei Tinoush T Botos Istvan I Ziółkowska Natasza E NE Bokesch Heidi R HR Krumpe Lauren R LR McKee Tawnya C TC O'Keefe Barry R BR Dauter Zbigniew Z Wlodawer Alexander A
Protein science : a publication of the Protein Society 20071026 12
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 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure ...[more]