N. Schiering et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM-DIPHTHERIAE, Journal of Molecular Biology, 244(5), 1994, pp. 654-656
Crystals of the diphtheria tox repressor (DtxR) from Corynebacterium d
iphtheriae suitable for structure determination have been obtained. Dt
xR activated with transition metal ions represses the expression of th
e structural gene for the diphtheria toxin, tox, which is encoded on t
he genome of a family of closely related corynebacteriophages. The spa
ce group of the obtained crystals is trigonal P3(1)21 or its enantiomo
rph P3(2)21 with a = b = 64.2 Angstrom, c = 220.5 Angstrom, alpha = be
ta = 90 degrees, gamma = 120 degrees. Two monomers comprise the asymme
tric unit. The crystals diffract to a resolution of better than 3 Angs
trom.