Crystallization and preliminary X-ray studies of the diphtheria Tox repressor from Corynebacterium diphtheriae. Academic Article uri icon

Overview

abstract

  • Crystals of the diphtheria tox repressor (DtxR) from Corynebacterium diphtheriae suitable for structure determination have been obtained. DtxR activated with transition metal ions represses the expression of the structural gene for the diphtheria toxin, tox, which is encoded on the genome of a family of closely related corynebacteriophages. The space group of the obtained crystals is trigonal P3(1)21 or its enantiomorph P3(2)21 with a = b = 64.2 A, c = 220.5 A, alpha = beta = 90 degrees, gamma = 120 degrees. Two monomers comprise the asymmetric unit. The crystals diffract to a resolution of better than 3 A.

publication date

  • December 16, 1994

Research

keywords

  • Bacterial Proteins
  • Corynebacterium diphtheriae
  • DNA-Binding Proteins

Identity

Scopus Document Identifier

  • 0027937721

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1994.1760

PubMed ID

  • 7990147

Additional Document Info

volume

  • 244

issue

  • 5