Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering


Authors: 
Papageorgiou Nicolas, Lichière Julie, Baklouti Amal, Ferron François, Sévajol Marion, Canard Bruno, Coutard Bruno
Date of publication: 
Monday, 1 February, 2016
Volume: 
72
Issue: 
2
Pages: 
192-202
EVAg connections: 
Research funded by EVAg
Related to EVAg product
Published by EVAg partner

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100P-EVAg1595
N-terminal domain of the MERS CoV nucleocapsid (1-164). Pure recombinant protein produced in E. coli. resuspended in HEPES buffer 10 mM pH 7.5, NaCl 300 mM.
Unit: > 2 mg of protein
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Produced by:
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100P-EVAg1594
N-terminal domain of the MERS CoV nucleocapsid (37-164, without the N-terminal intrinsically disordered region. Pure recombinant protein produced in E. coli. resuspended in HEPES buffer 10 mM pH 7.5, NaCl 300 mM
Unit: > 2 mg of purified protein
Virus name: 


800,00 €
(Cost per access for Academics)


Produced by:
AMU_b
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100N-EVAg1597
Expression plasmid for the N-terminal Domain of the MERS CoV Nucleocapsid coding sequence in fusion with a TRX/6-His tag encoding sequence at its 5'. For expression in E. coli
Unit: 2µg of DNA
Virus name: 


250,00 €
(Cost per access for Academics)


Produced by:
AMU_b
Shipping From:
Marseille - FR
Ref-SKU:
100N-EVAg1596
Expression plasmid for the Nterminal Domain of the MERS CoV Nucleocapsid coding sequence in fusion with a TRX/6-His tag encoding sequence at its 5'. For expression in E. coli
Unit: 2µg of DNA
Virus name: 


250,00 €
(Cost per access for Academics)