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Titolo:
Crystallization of a recombinant form of the complete sequence of human gamma-interferon: characterization by small-angle X-ray scattering, mass spectrometry and preliminary X-ray diffraction studies
Autore:
Budayova-Spano, M; Shepard, W; Schoot, B; Astier, JP; Veesler, S;
Indirizzi:
CNRS, CRMC2, Ctr Rech Mecanismes Croissance Cristalline, F-13288 Marseille, France CNRS Marseille France F-13288 nce Cristalline, F-13288 Marseille, France Ctr Univ Paris Sud, LURE, F-91898 Orsay, France Ctr Univ Paris Sud OrsayFrance F-91898 Sud, LURE, F-91898 Orsay, France Aventis, F-93235 Romainville, France Aventis Romainville France F-93235Aventis, F-93235 Romainville, France
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 6
pagine: 900 - 905
SICI:
0907-4449(200106)57:<900:COARFO>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN IMMUNE INTERFERON; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; RECEPTOR-BINDING; EXPRESSION; LYSOZYME; TERMINUS; PROTEIN; PEPTIDE; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Veesler, S CNRS, CRMC2, Ctr Rech Mecanismes Croissance Cristalline, CampusLuminy,Case 913, F-13288 Marseille, France CNRS Campus Luminy,Case 913 Marseille France F-13288 e, France
Citazione:
M. Budayova-Spano et al., "Crystallization of a recombinant form of the complete sequence of human gamma-interferon: characterization by small-angle X-ray scattering, mass spectrometry and preliminary X-ray diffraction studies", ACT CRYST D, 57, 2001, pp. 900-905

Abstract

The crystallization conditions of a recombinant form of the complete sequence of human gamma -interferon, designated r-hu IFN-gamma (RU 42369), have been determined after studying the behaviour of this protein in solution bysmall-angle X-ray scattering (SAXS) as a function of pH and salt type. IFN-gamma is difficult to crystallize without truncating at least the last five amino acids of the C-terminus; the SAXS results suggest viable crystallization conditions that led to crystals of r-hu IFN-gamma suitable for X-ray diffraction analysis. The crystals were grown in the presence of ammonium sulfate using vapour-diffusion techniques. The crystals, which diffract to 5Angstrom resolution at best, belong to the primitive tetragonal space group P42(1)2 and have unit-cell parameters a = b = 123.4, c = 93.4 Angstrom. The protein contained in these crystals was analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), which verified the presence of the complete amino-acid sequence of r-hu IFN-gamma.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 21:38:33