Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 25-28 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 64 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2008 |
| MoE publication type | A1 Journal article-refereed |
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Keywords
- Antibodies
- Food allergens
- IgE
- Mass spectrometry
Cite this
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Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen. / Niemi, M.; Jänis, J.; Jylhä, Sirpa; Kallio, J. M.; Hakulinen, Nina; Laukkanen, Marja-Leena; Takkinen, Kristiina; Rouvinen, Juha.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64, No. 1, 2008, p. 25-28.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen
AU - Niemi, M.
AU - Jänis, J.
AU - Jylhä, Sirpa
AU - Kallio, J. M.
AU - Hakulinen, Nina
AU - Laukkanen, Marja-Leena
AU - Takkinen, Kristiina
AU - Rouvinen, Juha
PY - 2008
Y1 - 2008
N2 - A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT-ICR mass spectrometry and crystallized with bovine [beta]-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 Å resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 Å. The three-dimensional structure of the D1 Fab fragment-BLG complex will provide the first insight into IgE antibody-allergen interactions at the molecular level.
AB - A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT-ICR mass spectrometry and crystallized with bovine [beta]-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 Å resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 Å. The three-dimensional structure of the D1 Fab fragment-BLG complex will provide the first insight into IgE antibody-allergen interactions at the molecular level.
KW - Antibodies
KW - Food allergens
KW - IgE
KW - Mass spectrometry
U2 - 10.1107/S174430910706160X
DO - 10.1107/S174430910706160X
M3 - Article
VL - 64
SP - 25
EP - 28
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - 1
ER -