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Crystallization and Preliminary X-ray Analysis of Der f 2, a Potent Allergen Derived from the House Dust MiteAlthough a number of allergens have been identified and isolated, the underlying molecular basis for the potent immune response is poorly understood. House dust mites (Dermatophugoides sp.) are particularly ubiquitous contributors to atopy in developed countries. The rhinitis, dermatitis, and asthma associated with allergic reactions to these arthropods are often caused by relatively small (125-129 amino acids) mite proteins of unclear biological function. Der f 2, a major allergen from the mite Dermatophagoides farinae, has been recombinantly expressed and characterized. The Der f 2 protein has been crystallized in our laboratory and a native data set collected at a synchrotron source. The crystals belong to the orthorhombic space group I422 with unit cell parameters of a = 95.2 Angstroms, b = 95.2 Angstroms, and c = 103.3 Angstroms. An essentially complete (97.2%) data set has been collected to 2.4 Angstroms. Attempts to solve the crystal structure of Der f 2 by molecular replacement using the available NMR coordinates for either Der f 2 or Der p 2 (the homologous protein from D. pterovssinus) failed to reveal a creditable solution.
Document ID
20030002522
Document Type
Preprint (Draft being sent to journal)
Authors
Roeber, Dana (NASA Marshall Space Flight Center Huntsville, AL United States)
Achari, Aniruddha (NASA Marshall Space Flight Center Huntsville, AL United States)
Takai, Toshiro (Asahi Breweries, Ltd. Ibaraki, Japan)
Okumura, Yasushi (Asahi Breweries, Ltd. Ibaraki, Japan)
Scott, David L. (Massachusetts General Hospital Boston, MA United States)
Curreri, Peter
Date Acquired
August 21, 2013
Publication Date
January 1, 2002
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.