Reference : The incorporation of a non-natural amino acid (aza-tryptophan) may help to crystallize a...

	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/62755

Title :	The incorporation of a non-natural amino acid (aza-tryptophan) may help to crystallize a protein and to solve its crystal structure. Application to bacteriophage lambda lysozyme.
Language :	English
Author, co-author :	Evrard, Christine [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie Physique et de Cristallographie - CPMC > >]
	Fastrez, Jacques [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie Physique et des Biopolymères - BIOP > >]
	Declercq, Jean-Paul [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie Physique et de Cristallographie - CPMC > >]
Publication date :	1999
Journal title :	Acta Crystallographica Section D-Biological Crystallography
Publisher :	Blackwell Publishing
Volume :	D55
Pages :	430-435
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0907-4449
City :	Oxford
Country :	United Kingdom
Abstract :	[en] Until now, wild-type bacteriophage lambda lysozyme had been impossible to crystallize. This difficulty could be overcome by the replacement of the four tryptophan residues by azatryptophans. Analysis of the intermolecular and intramolecular contacts in this modification allows understanding of the differences in behaviour between the native and modified molecules. Furthermore, this mutation was very useful for the creation of new heavy-atom binding sites and for the solution of the non-crystallographic symmetry, which is extremely important for phase improvement. This procedure seems to be generally applicable, at least in the search for new possibilities for heavy-atom binding sites.
Permalink :	http://hdl.handle.net/2268/62755

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