Structure of an N-Terminal Truncated Form of Nendou (NSP15) From SARS-CORONAVIRUS

Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch.

0.2 M sodium bromide, 0.1 M sodium acetate, PH 5.5 and 25% PEG 2000MME, VAPOR DIFFUSION, SITTING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

THE FULL LENGTH ENZYME FOLDS AS AN OBLIGATE HEXAMER. THIS TRUNCATED PROTEIN IS STRUCTURED AS A MONOMER IN CRYSTALS AS WELL AS IN SOLUTION

ENDONUCLEASE NENDOU, RIBONUCLEASE, HOMOLOG OF XENOPUS XENDOU, SARS NSP15, N-TERMINAL TRUNCATED CONSTRUCT, Viral Protein