Crystal structure of Vibrio cholerae HutX protein / 第二军医大学学报
Academic Journal of Second Military Medical University
;
(12): 969-974, 2012.
Article
Dans Chinois
| WPRIM
| ID: wpr-839817
ABSTRACT
Objective To obtain purified Vibrio cholerae HutX and its diffraction data. Methods Protein HutX was obtained by gene cloning and protein expression, purified by nickcl sepharose affinity chromatography, anion exchange chromatography (source Q), and molecular sieve chromatography (Superdex 200), and identified by Western blotting analysis. Then the obtained protein was subjected to crystallization condition screening and hanging drop optimization. The obtained crystal structure was analyzed by X-ray diffraction method. Results Western blotting analysis indirectly indicated that the obtained protein was HutX protein. Then the HutX crystal and its diffraction data were obtained in the present study. Conclusion The findings of the present study pave a way for future research on the crystal structure and function of HutX protein and its role in heme utilization of Vibrio cholerae.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Type d'étude:
Étude pronostique
langue:
Chinois
Texte intégral:
Academic Journal of Second Military Medical University
Année:
2012
Type:
Article
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