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 |
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Format: | Artikel |
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. |
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ISSN: | 1063-7745 1562-689X |
DOI: | 10.1134/S106377452206027X |