Crystallization and preliminary X-ray analysis of a bacterial lysozyme produced by Streptomyces globisporus.
The extracellular bacteriolytic enzyme produced by Streptomyces globisporus shows a beta-1,4-N,6-O-diacetylmuramidase activity as well as a beta-1,4-N-acetylmuramidase activity. Crystals of this enzyme have been obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. They belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = 63.11 (4), c = 121.1 (1) A, diffract to at least 2.0 A resolution and are suitable for high-resolution structure analysis. The crystal structure was solved by molecular replacement using lysozyme produced by S. erythraeus as a search model. The structure refinement is now in progress.
Shiba
T
T
Graduate School of Pharmaceutical Sciences, University of Tokyo, 3-1, 7-Chome, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Harada
S
S
Sugawara
H
H
Naitow
H
H
Kai
Y
Y
Satow
Y
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D013291:Streptococcus / Q000201:enzymology*
D009113:Muramidase