Please use this identifier to cite or link to this item:
標題: Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein
作者: Chen, I.J.
Chou, C.C.
Liu, C.L.
Lee, C.C.
Kan, L.S.
Hou, M.H.
關鍵字: respiratory syndrome coronavirus;virus;sars;infections;stability;sequence;rna
Project: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
期刊/報告no:: Acta Crystallographica Section F-Structural Biology and Crystallization Communications, Volume 66, Page(s) 815-818.
The N-terminal domain of nucleocapsid protein from human coronavirus OC43 (HCoV-OC43 N-NTD) mostly contains positively charged residues and has been identified as being responsible for RNA binding during ribonucleocapsid formation in the coronavirus. In this study, the crystallization and preliminary crystallographic analysis of HCoV-OC43 N-NTD (amino acids 58-195) with a molecular weight of 20 kDa are reported. HCoV-OC43 N-NTD was crystallized at 293 K using PEG 1500 as a precipitant and a 99.9% complete native data set was collected to 1.7 angstrom resolution at 100 K with an overall R(merge) of 5.0%. The crystals belonged to the hexagonal space group P6(5), with unit-cell parameters a = 81.57, c = 42.87 angstrom. Solvent-content calculations suggest that there is likely to be one subunit of N-NTD in the asymmetric unit.
ISSN: 1744-3091
DOI: 10.1107/s1744309110017616
Appears in Collections:期刊論文

Show full item record

Google ScholarTM




Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.