title: Preliminary crystallographic analysis of a complex between tetracycline and the trypsin-modified form of Escherichia coli elongation factor Tu.
abstract: 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 beta = 95.3 degrees, and contain six molecules of the complex per asymmetric unit. The crystals are well ordered and diffract to a resolution of 2.3 A.
authors.affiliation: Department of Biochemistry, University of California, Riverside 92521.
authors.forename: S
authors.initials: S
authors.lastname: Mui
authors.forename: K
authors.initials: K
authors.lastname: Delaria
authors.forename: F
authors.initials: F
authors.lastname: Jurnak
mesh_terms: D004926:Escherichia coli; D010444:Peptide Elongation Factor Tu; D013752:Tetracycline; D014357:Trypsin / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D014357:Trypsin; D010444:Peptide Elongation Factor Tu; D013752:Tetracycline