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Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein
Author(s) -
Wang YongSheng,
Chang Chungke,
Hou MingHon
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15010146
Subject(s) - monoclinic crystal system , middle east respiratory syndrome coronavirus , crystallization , crystallography , virology , middle east respiratory syndrome , coronavirus , chemistry , biology , microbiology and biotechnology , crystal structure , medicine , covid-19 , disease , organic chemistry , pathology , infectious disease (medical specialty)
The N‐terminal domain of the nucleocapsid protein from Middle East respiratory syndrome coronavirus (MERS‐CoV NP‐NTD) contains many positively charged residues and has been identified to be responsible for RNA binding during ribonucleocapsid formation by the virus. In this study, the crystallization and crystallographic analysis of MERS‐CoV NP‐NTD (amino acids 39–165), with a molecular weight of 14.7 kDa, are reported. MERS‐CoV NP‐NTD was crystallized at 293 K using PEG 3350 as a precipitant and a 94.5% complete native data set was collected from a cooled crystal at 77 K to 2.63 Å resolution with an overall R merge of 9.6%. The crystals were monoclinic and belonged to space group P 2 1 , with unit‐cell parameters a = 35.60, b = 109.64, c = 91.99 Å, β = 101.22°. The asymmetric unit contained four MERS‐CoV NP‐NTD molecules.