Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Dependence of nucleation kinetics and crystal morphology of a model protein system on ionic strength
Autore:
Bhamidi, V; Skrzypczak-Jankun, E; Schall, CA;
Indirizzi:
Univ Toledo, Dept Chem & Environm Engn, Toledo, OH 43606 USA Univ Toledo Toledo OH USA 43606 hem & Environm Engn, Toledo, OH 43606 USA Univ Toledo, Instrumentat Ctr, Toledo, OH 43606 USA Univ Toledo Toledo OHUSA 43606 o, Instrumentat Ctr, Toledo, OH 43606 USA
Titolo Testata:
JOURNAL OF CRYSTAL GROWTH
fascicolo: 1-4, volume: 232, anno: 2001,
pagine: 77 - 85
SICI:
0022-0248(200111)232:1-4<77:DONKAC>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOZYME SOLUTIONS; CRYSTALLIZATION; GROWTH; FORM; PH;
Keywords:
nucleation; growth from solutions; lysozyme; proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
--discip_EC--
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Schall, CA Univ Toledo, Dept Chem & Environm Engn, 2801 W Bancroft St, Toledo, OH 43606 USA Univ Toledo 2801 W Bancroft St Toledo OH USA 43606 OH 43606 USA
Citazione:
V. Bhamidi et al., "Dependence of nucleation kinetics and crystal morphology of a model protein system on ionic strength", J CRYST GR, 232(1-4), 2001, pp. 77-85

Abstract

Nucleation rate data for hen egg-white lysozyme crystallization were obtained using a particle counter. Tetragonal lysozyme crystals were expected toform at the temperature and solution conditions of these experiments: 4 degreesC, pH 4.5 with 0.1 M sodium acetate buffer and 2-6% NaCl (w/v). The rates varied as expected, as smooth monotonic functions of supersaturation at2%, 3% and 6% NaCl. However, at 5% NaCl, a great deal of scatter in the data was observed. At 2% and 3% NaCl, all the batches contained crystals withtetragonal morphology. At 6% NaCl, almost all of the vials contained the white powder with few or no tetragonal crystals. At 5% NaCl concentration, amixture of tetragonal crystals and powder formed in varying proportions inall the vials as observed by visual inspection. The powdery material was examined using optical microscopy and was seen to consist of needles with regular structure and sharp, faceted edges. Powder diffraction data from these needles was inconsistent with experimental powder diffraction data from tetragonal lysozyme crystals. It is possible that at high salt and protein concentrations liquid-liquid separation occurred and yielded a crystal polymorph. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:15:48