Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans.

Evrard, Charles-Marie;Declercq, Jean-Paul;Fastrez, Jacques
(1997) Acta crystallographica. Section D, Biological crystallography — Vol. 53, n° Pt 2, p. 217-219 (1997)

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  • Evrard, Charles-MarieUCLouvain
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  • Declercq, Jean-PaulUCLouvain
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  • Fastrez, JacquesUCLouvain
    Author
Abstract
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unsuccessful attempts to crystallize the bacteriophage lambda lysozyme, a mutant where all the tryptophan residues have been replaced by aza-tryptophans has been crystallized by the vapor-diffusion method.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 P2(1)2(1)2(1) with cell dimensions a = 73.01, b = 78.80, c = 82.31 A. Diffraction data were collected using synchrotron radiation sources. Crystals diffract to a resolution of 2.3 A. Data from two different platinum derivatives were also recorded to 2.8 and 2.5 A, respectively.
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Evrard, C.-M., Declercq, J.-P., & Fastrez, J. (1997). Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans. Acta crystallographica. Section D, Biological crystallography, 53(Pt 2), 217-219. https://doi.org/10.1107/S0907444996011523 (Original work published 1997)