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

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. Cryst...

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Veröffentlicht in:Crystallography reports 2023-02, Vol.68 (1), p.52-56
Hauptverfasser: Timofeev, V. I., Abramchik, Yu. A., Zhukhlistova, N. E., Mikheeva, O. O., Shevtsov, M. B., Zayats, E. A., Lykoshin, D. D., Kostromina, M. A., Esipov, R. S., Kuranova, I. P.
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Sprache:eng
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Zusammenfassung: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. С 121 and contain two enzyme molecules per asymmetric unit.
ISSN:1063-7745
1562-689X
DOI:10.1134/S106377452206027X