Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment

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Standard

Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment. / Spangfort, M D; Mirza, Osman Asghar; Gajhede, M.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 55, No. Pt 12, 12.1999, p. 2035-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Spangfort, MD, Mirza, OA & Gajhede, M 1999, 'Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment', Acta Crystallographica. Section D: Biological Crystallography, vol. 55, no. Pt 12, pp. 2035-6.

APA

Spangfort, M. D., Mirza, O. A., & Gajhede, M. (1999). Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment. Acta Crystallographica. Section D: Biological Crystallography, 55(Pt 12), 2035-6.

Vancouver

Spangfort MD, Mirza OA, Gajhede M. Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment. Acta Crystallographica. Section D: Biological Crystallography. 1999 Dec;55(Pt 12):2035-6.

Author

Spangfort, M D ; Mirza, Osman Asghar ; Gajhede, M. / Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment. In: Acta Crystallographica. Section D: Biological Crystallography. 1999 ; Vol. 55, No. Pt 12. pp. 2035-6.

Bibtex

@article{781b9e51a8ae4c9d86c3b25394e65a1b,
title = "Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment",
abstract = "The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 A, alpha = 105.7, beta = 98.32, gamma = 97.62 degrees, and diffract to 2.9 A resolution when analyzed at 100 K using synchrotron-generated X--rays.",
keywords = "Allergens, Animals, Antibodies, Monoclonal, Antigen-Antibody Reactions, Antigens, Plant, Crystallization, Crystallography, X-Ray, Humans, Immunoglobulin Fab Fragments, Immunoglobulin G, Mice, Plant Proteins, Pollen, Rhinitis, Allergic, Seasonal",
author = "Spangfort, {M D} and Mirza, {Osman Asghar} and M Gajhede",
year = "1999",
month = dec,
language = "English",
volume = "55",
pages = "2035--6",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 12",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment

AU - Spangfort, M D

AU - Mirza, Osman Asghar

AU - Gajhede, M

PY - 1999/12

Y1 - 1999/12

N2 - The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 A, alpha = 105.7, beta = 98.32, gamma = 97.62 degrees, and diffract to 2.9 A resolution when analyzed at 100 K using synchrotron-generated X--rays.

AB - The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 A, alpha = 105.7, beta = 98.32, gamma = 97.62 degrees, and diffract to 2.9 A resolution when analyzed at 100 K using synchrotron-generated X--rays.

KW - Allergens

KW - Animals

KW - Antibodies, Monoclonal

KW - Antigen-Antibody Reactions

KW - Antigens, Plant

KW - Crystallization

KW - Crystallography, X-Ray

KW - Humans

KW - Immunoglobulin Fab Fragments

KW - Immunoglobulin G

KW - Mice

KW - Plant Proteins

KW - Pollen

KW - Rhinitis, Allergic, Seasonal

M3 - Journal article

C2 - 10666582

VL - 55

SP - 2035

EP - 2036

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 12

ER -

ID: 44864122