Crystallization and preliminary crystallographic data of a Fel d 1 (1+2) construct corresponding to the major allergen from cat.
The domestic cat (Felis domesticus) is one of the most important causes of allergic disease worldwide. A homologue of the major allergen Fel d 1 was created by linking the two chains that compose the protein. Fel d 1 (1+2) was expressed in Escherichia coli and subsequently purified using three chromatographic steps. Crystals of Fel d 1 (1+2) were obtained using the hanging-drop vapour-diffusion method in 22.5% PEG 3350, 0.5 M CaCl2. The crystals belong to space group P1, with unit-cell parameters a = 38.5, b = 42.9, c = 49.0 A, alpha = 70.7, beta = 80.5, gamma = 81.5 degrees , and diffract to 1.6 A resolution.
Kaiser
Liselotte
L
Center for Infectious Medicine, F59, Department of Medicine, Karolinska Institutet, Karolinska University Hospital Huddinge, 141 86 Stockholm, Sweden. liselotte.kaiser@medhs.ki.se
Grönlund
Hans
H
van Hage-Hamsten
Marianne
M
Achour
Adnane
A
D000485:Allergens; D000818:Animals; D002415:Cats / Q000276:immunology*; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D000485:Allergens; D006023:Glycoproteins; D011994:Recombinant Proteins; C059296:Fel d 1 protein, Felis domesticus