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

Research output: Contribution to journalArticleScientificpeer-review

9 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 languageEnglish
Pages (from-to)25-28
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number1
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

Fingerprint

Lactoglobulins
Immunoglobulin Fab Fragments
Crystallization
antibodies
Allergens
Immunoglobulin E
fragments
crystallization
Synchrotrons
Antibodies
Synchrotron radiation
Mass spectrometry
Mass Spectrometry
synchrotron radiation
mass spectroscopy
Vapors
X-Rays
vapors
Radiation
X rays

Keywords

  • Antibodies
  • Food allergens
  • IgE
  • Mass spectrometry

Cite this

@article{ed875a67fd154f3b82e517cb94c9a1fa,
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",
volume = "64",
pages = "25--28",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "International Union of Crystallography",
number = "1",

}

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 journalArticleScientificpeer-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 -