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

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

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.

Original language	English
Pages (from-to)	573-579
Number of pages	7
Journal	Journal of Crystal Growth
Volume	232
Issue number	1-4
DOIs	https://doi.org/10.1016/S0022-0248(01)01205-2
Publication status	Published - 1 Nov 2001
Externally published	Yes

Keywords

A1. biocrystallization
A1. screening
B1. antibodies
B1. biological macromolecules

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0022-0248(01)01205-2

Cite this

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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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T1 - Crystallization of macromolecular complexes

T2 - Combinatorial complex crystallization

AU - Stura, Enrico A.

AU - Graille, Marc

AU - Charbonnier, Jean Baptiste

PY - 2001/11/1

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

AN - SCOPUS:0035501917

SN - 0022-0248

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

Abstract

Keywords

UN SDGs

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