• Citer

The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.

par Van Molle, Inge;Moonens, Kristof;Buts, Lieven;Garcia-Pino, Abel ;Panjikar, Santosh;Wyns, Lode;De Greve, Henri;Bouckaert, Julie
Référence Acta crystallographica. Section D, Biological crystallography, 65, Pt 5, page (411-420)
Publication Publié, 2009-05

Article révisé par les pairs

• Détails
• Contenu

Titre:	The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.
Auteur:	Van Molle, Inge; Moonens, Kristof; Buts, Lieven; Garcia-Pino, Abel; Panjikar, Santosh; Wyns, Lode; De Greve, Henri; Bouckaert, Julie
Informations sur la publication:	Acta crystallographica. Section D, Biological crystallography, 65, Pt 5, page (411-420)
Statut de publication:	Publié, 2009-05
Sujet CREF:	Sciences bio-médicales et agricoles
MeSH keywords:	Adhesins, Escherichia coli -- chemistry
	Calorimetry, Differential Scanning
	Cross-Linking Reagents -- pharmacology
	Crystallography, X-Ray
	Dimerization
	Escherichia coli -- chemistry -- genetics
	Escherichia coli Proteins -- chemistry -- genetics -- isolation & purification -- metabolism
	Fimbriae Proteins -- metabolism
	Glutaral -- pharmacology
	Models, Molecular
	Molecular Chaperones -- chemistry -- genetics -- isolation & purification -- metabolism
	Nephelometry and Turbidimetry
	Protein Conformation
	Protein Denaturation
	Protein Interaction Mapping
	Recombinant Fusion Proteins -- chemistry -- isolation & purification
Note générale:	FLWNA
Langue:	Anglais
Identificateurs:	urn:issn:0907-4449
	info:doi/10.1107/S0907444909005174
	info:pii/S0907444909005174
	info:pmid/19390146