Crystallization and Preliminary X-ray Studies of the Diphtheria Tox Repressor from Corynebacterium diphtheriae
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 famil...
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Veröffentlicht in: | Journal of molecular biology 1994-12, Vol.244 (5), p.654-656 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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
121 or its enantiomorph P3
221 with
a =
b = 64.2 Å,
c = 220.5 Å, α = β = 90°, γ = 120°. Two monomers comprise the asymmetric unit. The crystals diffract to a resolution of better than 3 Å. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1006/jmbi.1994.1760 |