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Updated: Aug 11, 2026
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Crystallization and preliminary crystallographic data of a Fel d 1 (1+2) construct corresponding to the major
Liselotte Kaiser1, Hans Grönlund, Marianne van Hage-Hamsten
1Center for Infectious Medicine, F59, Department of Medicine, Karolinska Institutet, Karolinska University Hospital Huddinge, 141 86 Stockholm, Sweden. liselotte.kaiser@medhs.ki.se
Abstract:
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.
