Article (Scientific journals)
Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans
Evrard, Christine; Declercq, Jean-Paul; Fastrez, Jacques
1997In Acta Crystallographica. Section D, Biological Crystallography, D53, p. 217-219
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Abstract :
[en] After many unsuccessful attempts to crystallize the bacteriophage lambda lysozyme, a mutant where all the tryptophan residues have been replaced by aza-tryptophans has been crystallized by the vapor-diffusion method. The crystals are orthorhombic and belong to space group P212121 with cell dimensions a = 73.01, b = 78.80, c = 82.31 Å. Diffraction data were collected using synchrotron radiation sources. Crystals diffract to a resolution of 2.3 Å. Data from two different platinum derivatives were also recorded to 2.8 and 2.5 Å, respectively.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Evrard, Christine ;  Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie physique et de Cristallographie - Laboratoire de Biochimie Physique et des Biololymères
Declercq, Jean-Paul;  Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie Physique et de Cristallographie
Fastrez, Jacques;  Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie physique et des biopolymères
Language :
English
Title :
Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans
Publication date :
1997
Journal title :
Acta Crystallographica. Section D, Biological Crystallography
ISSN :
0907-4449
eISSN :
1399-0047
Publisher :
Blackwell Publishing, Oxford, United Kingdom
Volume :
D53
Pages :
217-219
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 June 2010

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