ObjectiveTo obtain purified Vibrio cholerae HutX and its diffraction data. MethodsProtein 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. ResultsWestern 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. ConclusionThe 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.