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Titolo:
CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDY OF AN IDIOTOPE-ANTI-IDIOTOPE FV-FV COMPLEX
Autore:
GOLDBAUM FA; FIELDS BA; CAUERHFF A; YSERN X; HOUDUSSE A; EISELE JL; POLJAK RJ; MARIUZZA RA;
Indirizzi:
UNIV MARYLAND,MARYLAND BIOTECHNOL INST,CTR ADV RES BIOTECHNOL,9600 GUDELSKY DR ROCKVILLE MD 20850 UNIV MARYLAND,MARYLAND BIOTECHNOL INST,CTR ADV RES BIOTECHNOL ROCKVILLE MD 20850 NIST ROCKVILLE MD 20850 US FDA,CTR DRUG EVALUAT & RES ROCKVILLE MD 20857 INST PASTEUR F-75724 PARIS FRANCE
Titolo Testata:
Journal of Molecular Biology
fascicolo: 5, volume: 241, anno: 1994,
pagine: 739 - 743
SICI:
0022-2836(1994)241:5<739:CAPDSO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN VARIABLE DOMAINS; SITE-DIRECTED MUTAGENESIS; 3-DIMENSIONAL STRUCTURE; BINDING; ANTIBODIES; RECOGNITION; LYSOZYME; PROTEINS; CONTACT; SURFACE;
Keywords:
FV FRAGMENT; IDIOTOPE CRYSTALLIZATION; X-RAY ANALYSIS;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
F.A. Goldbaum et al., "CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDY OF AN IDIOTOPE-ANTI-IDIOTOPE FV-FV COMPLEX", Journal of Molecular Biology, 241(5), 1994, pp. 739-743

Abstract

A complex between the Fv fragment of an anti-hen eggwhite lysozyme antibody (D1.3) and the Fv fragment of an antibody specific for an idiotypic determinant of D1.3 has been crystallized in a form suitable for X-ray diffraction analysis. Both Fv fragments were expressed in soluble form in Escherichia coli and purified by affinity chromatography; diffraction-quality crystals were only obtained following separation of each Fv into distinct isoelectric forms. The crystals belong to space group C2, have unit cell dimensions a = 152.8 Angstrom, b = 79.4 Angstrom, c = 51.5 Angstrom, beta = 100.2 degrees, and diffract to better than 2.2 Angstrom resolution. The solvent content of the crystals is approximately 60% (v/v) with one Fv-Fv complex in the asymmetric unit. The ability to readily express both components of an antigen-antibody system in bacteria will allow us to rigorously assess the energetic contribution of individual amino acids to complex formation through pairwise mutagenesis of interacting residues.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 18:46:42