Preliminary crystallographic analysis of a complex between tetracycline and the trypsin-modified form of Escherichia coli elongation factor Tu

Crystals of a complex between the antibiotic tetracycline and the trypsin-modified form of the Escherichia coli protein elongation factor Tu have been grown in a form suitable for high-resolution X-ray diffraction analysis. The crystals belong to space group P2 1; with cell dimensions a = 69.7 A ̊ ,...

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Veröffentlicht in:Journal of molecular biology 1990-04, Vol.212 (3), p.445-447
Hauptverfasser: Mui, Suet, Delaria, Katherine, Jurnak, Frances
Format: Artikel
Sprache:eng
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Zusammenfassung:Crystals of a complex between the antibiotic tetracycline and the trypsin-modified form of the Escherichia coli protein elongation factor Tu have been grown in a form suitable for high-resolution X-ray diffraction analysis. The crystals belong to space group P2 1; with cell dimensions a = 69.7 A ̊ , b = 156.4 A ̊ , c = 135.4 A ̊ and β = 95.3 ° , and contain six molecules of the complex per asymmetric unit. The crystals are well ordered and diffract to a resolution of 2.3 Å.
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(90)90322-D