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Journal article

High-level bacterial expression and purification of apicomplexan micronemal proteins for structural studies.

Abstract:
The cysteine-rich N-terminal domain of the micronemal adhesive protein MIC1 (MIC1-NT) from Toxoplasma gondii was cloned, expressed in Escherichia coli and purified. MIC1-NT is amenable to structural studies as shown by preliminary NMR and X-ray analysis. Positive results with two further micronemal proteins indicate that our strategy has wider application.
Publication status:
Published

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Publisher copy:
10.2174/092986607780782876

Authors


Saouros, S More by this author
Blumenschein, TM More by this author
Sawmynaden, K More by this author
Marchant, J More by this author
Koutroukides, T More by this author
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Journal:
Protein and peptide letters
Volume:
14
Issue:
5
Pages:
411-415
Publication date:
2007
DOI:
EISSN:
1875-5305
ISSN:
0929-8665
URN:
uuid:ae80eb95-91da-49d7-9f78-36adc1ee7343
Source identifiers:
72836
Local pid:
pubs:72836

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