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Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Identifieur interne : 001494 ( Main/Exploration ); précédent : 001493; suivant : 001495

Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Auteurs : Yong-Sheng Wang ; Chung-Ke Chang ; Ming-Hon Hou

Source :

RBID : ISTEX:C3B5F5FB070CC05A15D0F4CB89100C34C7F2B621

Abstract

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 Rmerge of 9.6%. The crystals were monoclinic and belonged to space group P21, 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.

Url:
DOI: 10.1107/S2053230X15010146


Affiliations:


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