Work

Crystallization and Preliminary X-ray Studies of the Diphtheria Tox Repressor from Corynebacterium diphtheriae

Year: 1994

Type: article

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.

Source: Journal of Molecular Biology

DOI: 10.1006/jmbi.1994.1760

Authors: Nikolaus Schiering, Xu Tao, John R. Murphy, Gregory A. Petsko, Dagmar Ringe

Institution: Brandeis University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,730

Funder: National Institute of Allergy and Infectious Diseases