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

The high-producing strain C3029/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 & ANGS; resolution at the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K. The crystals belong to sp. gr. C121 and contain two enzyme molecules per asymmetric unit.

Automated summary

The high-producing strain C3029/pGro7/pERDerp3 expressing the recombinant allergen Der p 3 was constructed and purified. Crystals of the recombinant protein suitable for X-ray diffraction analysis were grown and the X-ray diffraction data set was collected. The crystals belong to sp. gr. C121 and contain two enzyme molecules per asymmetric unit.