Preparation, Crystallization, and Preliminary X-ray Diffraction Analysis of Recombinant House Dust Mite Allergen Der p 3 from Dermatophagoides pteronyssinus

V. I. Timofeev,Yu. A. Abramchik, N. E. Zhukhlistova, O. O. Mikheeva, M. B. Shevtsov, E. A. Zayats, D. D. Lykoshin, M. A. Kostromina,R. S. Esipov,I. P. Kuranova

Crystallography Reports(2023)

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摘要
The high-producing strain С3029/pGro7/pERDerp3 for the house dust mite allergen Der p 3 from Dermatophagoides pteronyssinus, expressing the recombinant protein in Escherichia coli in the soluble form, was constructed. A procedure was developed for the purification of the recombinant allergen. Crystals of the recombinant protein Der p 3 suitable for X-ray diffraction analysis were grown by the vapor-diffusion method. The X-ray diffraction data set was collected to 2.25 Å resolution at the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K. The crystals belong to sp. gr. С121 and contain two enzyme molecules per asymmetric unit.
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关键词
house dust mite,dermatophagoides pteronyssinus,crystallization,x-ray
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