Fa. Goldbaum et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF THE LUMAZINE SYNTHASE FROM BRUCELLA-ABORTUS, Journal of structural biology (Print), 123(2), 1998, pp. 175-178
Lumazine synthase from Brucella abortus was overexpressed in Escherich
ia coli, refolded, and purified to apparent homogeneity. Crystals of l
umazine synthase were grown by the hanging drop vapor diffusion method
using polyethylene glycol 8000 or ammonium sulfate as precipitants. T
hey belong to the trigonal space group P321 with cell parameters a = b
= 132.00 Angstrom, c = 167.25 Angstrom. A complete diffraction data s
et to 3.7 Angstrom resolution has been collected using synchrotron rad
iation. Preliminary analysis of the quaternary structure of this prote
in by means of a self-rotation function calculated with the diffractio
n data clearly indicates 532 symmetry compatible with the presence of
an icosahedral lumazine synthase particle. (C) 1998 Academic Press.