Crystallization of macromolecular complexes: Combinatorial complex crystallization

Enrico A. Stura; Marc Graille; Jean Baptiste Charbonnier

doi:10.1016/S0022-0248(01)01205-2

Crystallization of macromolecular complexes: Combinatorial complex crystallization

Enrico A. Stura
, Marc Graille
, Jean Baptiste Charbonnier

CEA/UVSQ/CNRS

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

7 Citations (Scopus)

Résumé

The structure of the Fab-staphylococcus aureus protein A (SpA) and Fab-peptostreptococcus magnus protein L (PpL) complexes was studied which was applied to a few ternary complexes. The use of Ig-biding proteins as a way of extending the method from HIV gp120 to all proteins for which there are monoclonal antibodies was also proposed. It was found that even with relatively unpurified samples, it was possible to discover crystallization. The results showed that Ig-binding proteins can positively influence the crystallization of Fab-antigen complexes.

langue originale	Anglais
Pages (de - à)	573-579
Nombre de pages	7
journal	Journal of Crystal Growth
Volume	232
Numéro de publication	1-4
Les DOIs	https://doi.org/10.1016/S0022-0248(01)01205-2
état	Publié - 1 nov. 2001
Modification externe	Oui

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title = "Crystallization of macromolecular complexes: Combinatorial complex crystallization",

abstract = "The structure of the Fab-staphylococcus aureus protein A (SpA) and Fab-peptostreptococcus magnus protein L (PpL) complexes was studied which was applied to a few ternary complexes. The use of Ig-biding proteins as a way of extending the method from HIV gp120 to all proteins for which there are monoclonal antibodies was also proposed. It was found that even with relatively unpurified samples, it was possible to discover crystallization. The results showed that Ig-binding proteins can positively influence the crystallization of Fab-antigen complexes.",

keywords = "A1. biocrystallization, A1. screening, B1. antibodies, B1. biological macromolecules",

author = "Stura, \{Enrico A.\} and Marc Graille and Charbonnier, \{Jean Baptiste\}",

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doi = "10.1016/S0022-0248(01)01205-2",

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AU - Stura, Enrico A.

AU - Graille, Marc

AU - Charbonnier, Jean Baptiste

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Y1 - 2001/11/1

N2 - The structure of the Fab-staphylococcus aureus protein A (SpA) and Fab-peptostreptococcus magnus protein L (PpL) complexes was studied which was applied to a few ternary complexes. The use of Ig-biding proteins as a way of extending the method from HIV gp120 to all proteins for which there are monoclonal antibodies was also proposed. It was found that even with relatively unpurified samples, it was possible to discover crystallization. The results showed that Ig-binding proteins can positively influence the crystallization of Fab-antigen complexes.

AB - The structure of the Fab-staphylococcus aureus protein A (SpA) and Fab-peptostreptococcus magnus protein L (PpL) complexes was studied which was applied to a few ternary complexes. The use of Ig-biding proteins as a way of extending the method from HIV gp120 to all proteins for which there are monoclonal antibodies was also proposed. It was found that even with relatively unpurified samples, it was possible to discover crystallization. The results showed that Ig-binding proteins can positively influence the crystallization of Fab-antigen complexes.

KW - A1. biocrystallization

KW - A1. screening

KW - B1. antibodies

KW - B1. biological macromolecules

U2 - 10.1016/S0022-0248(01)01205-2

DO - 10.1016/S0022-0248(01)01205-2

M3 - Article

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VL - 232

SP - 573

EP - 579

JO - Journal of Crystal Growth

JF - Journal of Crystal Growth

IS - 1-4

ER -

Crystallization of macromolecular complexes: Combinatorial complex crystallization

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