Reference : Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in wh...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63965
Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans
English
Evrard, Christine mailto [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 mailto [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie Physique et de Cristallographie > >]
Fastrez, Jacques mailto [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie physique et des biopolymères > >]
1997
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
D53
217-219
Yes (verified by ORBi)
International
0907-4449
Oxford
United Kingdom
[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unsuccessful attempts to crystallize the bacteriophage lambda lysozyme, a mutant where all the tryptophan residues have been replaced by aza-tryptophans has been crystallized by the vapor-diffusion method.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.
http://hdl.handle.net/2268/63965

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