Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen

M. Niemi; J. Jänis; Sirpa Jylhä; J. M. Kallio; Nina Hakulinen; Marja-Leena Laukkanen; Kristiina Takkinen; Juha Rouvinen

doi:10.1107/S174430910706160X

Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen

M. Niemi, J. Jänis, Sirpa Jylhä, J. M. Kallio, Nina Hakulinen, Marja-Leena Laukkanen, Kristiina Takkinen, Juha Rouvinen

University of Eastern Finland

Research output: Contribution to journal › Article › Scientific › peer-review

14 Citations (Scopus)

Abstract

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.

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	https://doi.org/10.1107/S174430910706160X
Publication status	Published - 2008
MoE publication type	A1 Journal article-refereed

Keywords

Antibodies
Food allergens
IgE
Mass spectrometry

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10.1107/S174430910706160X

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Niemi, M., Jänis, J., Jylhä, S., Kallio, J. M., Hakulinen, N., Laukkanen, M.-L., Takkinen, K., & Rouvinen, J. (2008). Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(1), 25-28. https://doi.org/10.1107/S174430910706160X

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title = "Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen",

abstract = "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 {\AA} 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 {\AA}. 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.",

keywords = "Antibodies, Food allergens, IgE, Mass spectrometry",

author = "M. Niemi and J. J{\"a}nis and Sirpa Jylh{\"a} and Kallio, {J. M.} and Nina Hakulinen and Marja-Leena Laukkanen and Kristiina Takkinen and Juha Rouvinen",

year = "2008",

doi = "10.1107/S174430910706160X",

language = "English",

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Niemi, M, Jänis, J, Jylhä, S, Kallio, JM, Hakulinen, N, Laukkanen, M-L, Takkinen, K & Rouvinen, J 2008, 'Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 1, pp. 25-28. https://doi.org/10.1107/S174430910706160X

Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen. / Niemi, M.; Jänis, J.; Jylhä, Sirpa et al.
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

SN - 1744-3091

VL - 64

SP - 25

EP - 28

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 1

ER -

Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen

Abstract

Keywords

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