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Figure 5
(a) Normalized Kratky plot of DENV-3 NS5FL (blue filled circles), MTase1–272 (red filled circles) and RdRp263–900 (brown filled circles) compared with the compact globular lysozyme (grey filled circles), with the expected peak (grey dashed line) representing the theoretical peak assuming an ideal Guinier region of a globular particle. Similar to DENV-3 NS5FL, MTase1–272 adopted a similar peak to DENV-3 NS5L, while RdRp263–900 had a peak at the theoretical peak for a globular protein, suggesting that the RdRp domain is slightly more rigid in solution when compared with the methyltransferase domain and full-length NS5 of DENV-3. (b) Porod–Debye plots (black circles) and fit lines (red) of DENV-3 NS5FL, MTase1–272 and RdRp263–900. The data for RdRp263–900 show a Porod–Debye plateau (Porod exponent = 4.0), while this plateau was absent for MTase1–272 (Porod exponent = 3.5), showing that the flexibility seen in DENV-3 NS5FL is partially driven by the methyltransferase domain and its linker.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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