Norwalk Virus polymerase bound to 5-nitrocytidine triphosphate and primer-template RNA

5-nitrocytidine 5'-(tetrahydrogen triphosphate)

5-nitrocytidine 5'-(dihydrogen phosphate)

Structural insights into mechanisms of catalysis and inhibition in norwalk virus polymerase.

White beam slits, cryo-cooled first and sagittally bent second crystal of double crystal monochromator (DCM), vertically focusing mirror (VFM)

sagittally bent second crystal of double crystal monochromator

RNA (5'-R(*UP*GP*CP*CP*CP*GP*GP*GP*(N5M))-3')

16% (w/v) PEG 8000, 25% (w/v) glycerol, 100 mM Tris-HCl, 50 mM KCl, 4 mM MgCl2, 10 mM MnCl2, 14 mM 2-mercaptoethanol, 0.1% (w/v) CHAPS, 0.5 mM RNA duplex, 1 mM NTP, 0.03 mM polymerase, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

chemically synthesized self-complementary RNA oligonucleotide with 2-base overhang

chemically synthesized self-complementary RNA oligonucleotide that was extended by a single 5-nitrocytidine monophosphate residue during crystallization

RNA-dependent RNA polymerase, viral replication, antiviral enzyme inhibitor, Helicase, Hydrolase, Nucleotide-binding, Nucleotidyltransferase, RNA replication, RNA-directed RNA polymerase, Transferase, Transferase-RNA COMPLEX