Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein.
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 A 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 A. Solvent-content calculations suggest that there is likely to be one subunit of N-NTD in the asymmetric unit.
Chen
I Jung
IJ
Department of Life Sciences, National Chung Hsing University, Taichung 402, Taiwan.
Chou
Chia Cheng
CC
Liu
Chia Ling
CL
Lee
Cheng Chung
CC
Kan
Lou Sing
LS
Hou
Ming Hon
MH
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D028962:Coronavirus OC43, Human / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D013696:Temperature
D019590:Nucleocapsid Proteins