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Titolo:
Structural effects of monovalent anions on polymorphic lysozyme crystals
Autore:
Vaney, MC; Broutin, I; Retailleau, P; Douangamath, A; Lafont, S; Hamiaux, C; Prange, T; Ducruix, A; Ries-Kautt, M;
Indirizzi:
Fac Pharm, Lab Cristallog & RMN Biol, CNRS, UMR 8015, F-75006 Paris, France Fac Pharm Paris France F-75006 ol, CNRS, UMR 8015, F-75006 Paris, France Ctr Univ Paris Sud, LURE, F-91898 Orsay, France Ctr Univ Paris Sud OrsayFrance F-91898 Sud, LURE, F-91898 Orsay, France
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 7
pagine: 929 - 940
SICI:
0907-4449(200107)57:<929:SEOMAO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
EGG-WHITE LYSOZYME; X-RAY; PROTEIN CRYSTALLIZATION; NEUTRON-DIFFRACTION; TRICLINIC LYSOZYME; REFINED STRUCTURES; ANOMALOUS SIGNAL; RESOLUTION; BINDING; CRYSTALLOGENESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Ries-Kautt, M Fac Pharm, Lab Cristallog & RMN Biol, CNRS, UMR 8015, 4 Ave Observ, F-75006 Paris, France Fac Pharm 4 Ave Observ Paris France F-75006 6 Paris, France
Citazione:
M.C. Vaney et al., "Structural effects of monovalent anions on polymorphic lysozyme crystals", ACT CRYST D, 57, 2001, pp. 929-940

Abstract

Understanding direct salt effects on protein crystal polymorphism is addressed by comparing different crystal forms (triclinic, monoclinic, tetragonal and orthorhombic) for hen, turkey, bob white quail and human lysozymes. Four new structures of hen egg-white lysozyme are reported: crystals grown in the presence of NapTS diffracted to 1.85 Angstrom, of NaI to 1.6 Angstrom, of NaNO3 to 1.45 Angstrom and of KSCN to 1.63 Angstrom. These new structures are compared with previously published structures in order to draw a mapping of the surface of different lysozymes interacting with monovalent anions, such as nitrate, chloride, iodide, bromide and thiocyanate. An analysis of the structural sites of these anions in the various lysozyme structures is presented. This study shows common anion sites whatever the crystal form and the chemical nature of anions, while others seem specific to a givengeometry and a particular charge environment induced by the crystal packing.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 21:41:00