Production, crystallization and preliminary crystallographic study of the major cat allergen Fel d 1.
The domestic cat (Felis domesticus) is an important cause of allergic disease worldwide. The major cat allergen 1 (Fel d 1) has been expressed in Escherichia coli, purified and refolded in a soluble form. Crystals of Fel d 1 were obtained in 13% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate pH 4.8. The Fel d 1 crystals belong to space group P2(1), with unit-cell parameters a = 43.3, b = 51.5, c = 67.7 A, and diffract to 1.9 A resolution.
Kaiser
Liselotte
L
Department of Medicine, Unit of Clinical Immunology and Allergy, Karolinska Institutet and Hospital, Stockholm, Sweden. liselotte.kaiser@ks.se
Grönlund
Hans
H
Sandalova
Tatyana
T
Ljunggren
Hans-Gustaf
HG
Schneider
Gunter
G
van Hage-Hamsten
Marianne
M
Achour
Adnane
A
D000485:Allergens / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D002415:Cats; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D000485:Allergens; D006023:Glycoproteins; D011994:Recombinant Proteins; C059296:Fel d 1 protein, Felis domesticus