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 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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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. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1016/0022-2836(90)90322-D |